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Database: UniProt
Entry: Q00955
LinkDB: Q00955
Original site: Q00955 
ID   ACAC_YEAST              Reviewed;        2233 AA.
AC   Q00955; D6W1J1;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   13-FEB-2019, entry version 203.
DE   RecName: Full=Acetyl-CoA carboxylase;
DE            Short=ACC;
DE            EC=6.4.1.2 {ECO:0000269|PubMed:12663926, ECO:0000269|PubMed:15079078};
DE   AltName: Full=Fatty acid synthetase 3;
DE   AltName: Full=mRNA transport-defective protein 7;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACC1; Synonyms=ABP2, FAS3, MTR7; OrderedLocusNames=YNR016C;
GN   ORFNames=N3175;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2015-2022.
RX   PubMed=1350093; DOI=10.1073/pnas.89.10.4534;
RA   Al-Feel W., Chirala S.S., Wakil S.J.;
RT   "Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-
RT   CoA carboxylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4534-4538(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=6108218;
RA   Mishina M., Roggenkamp R., Schweizer E.;
RT   "Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin:
RT   apocarboxylase ligase.";
RL   Eur. J. Biochem. 111:79-87(1980).
RN   [5]
RP   FUNCTION.
RX   PubMed=6103540; DOI=10.1073/pnas.77.4.1814;
RA   Roggenkamp R., Numa S., Schweizer E.;
RT   "Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in
RT   acetyl-CoA carboxylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:1814-1817(1980).
RN   [6]
RP   INDUCTION.
RX   PubMed=1359536; DOI=10.1073/pnas.89.21.10232;
RA   Chirala S.S.;
RT   "Coordinated regulation and inositol-mediated and fatty acid-mediated
RT   repression of fatty acid synthase genes in Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10232-10236(1992).
RN   [7]
RP   INDUCTION.
RX   PubMed=8098706;
RA   Hasslacher M., Ivessa A.S., Paltauf F., Kohlwein S.D.;
RT   "Acetyl-CoA carboxylase from yeast is an essential enzyme and is
RT   regulated by factors that control phospholipid metabolism.";
RL   J. Biol. Chem. 268:10946-10952(1993).
RN   [8]
RP   ACTIVITY REGULATION.
RX   PubMed=7916271; DOI=10.1007/BF00309532;
RA   Vahlensieck H.F., Pridzun L., Reichenbach H., Hinnen A.;
RT   "Identification of the yeast ACC1 gene product (acetyl-CoA
RT   carboxylase) as the target of the polyketide fungicide soraphen A.";
RL   Curr. Genet. 25:95-100(1994).
RN   [9]
RP   INDUCTION.
RX   PubMed=8127678; DOI=10.1093/nar/22.3.412;
RA   Chirala S.S., Zhong Q., Huang W., al-Feel W.;
RT   "Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae:
RT   identification of a functional UASINO and sequences responsible for
RT   fatty acid mediated repression.";
RL   Nucleic Acids Res. 22:412-418(1994).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8943372; DOI=10.1128/MCB.16.12.7161;
RA   Schneiter R., Hitomi M., Ivessa A.S., Fasch E.V., Kohlwein S.D.,
RA   Tartakoff A.M.;
RT   "A yeast acetyl coenzyme A carboxylase mutant links very-long-chain
RT   fatty acid synthesis to the structure and function of the nuclear
RT   membrane-pore complex.";
RL   Mol. Cell. Biol. 16:7161-7172(1996).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9438137;
RA   Ivessa A.S., Schneiter R., Kohlwein S.D.;
RT   "Yeast acetyl-CoA carboxylase is associated with the cytoplasmic
RT   surface of the endoplasmic reticulum.";
RL   Eur. J. Cell Biol. 74:399-406(1997).
RN   [12]
RP   FUNCTION.
RX   PubMed=10757783; DOI=10.1128/MCB.20.9.2984-2995.2000;
RA   Schneiter R., Guerra C.E., Lampl M., Tatzer V., Zellnig G.,
RA   Klein H.L., Kohlwein S.D.;
RT   "A novel cold-sensitive allele of the rate-limiting enzyme of fatty
RT   acid synthesis, acetyl coenzyme A carboxylase, affects the morphology
RT   of the yeast vacuole through acylation of Vac8p.";
RL   Mol. Cell. Biol. 20:2984-2995(2000).
RN   [13]
RP   FUNCTION.
RX   PubMed=12730220; DOI=10.1074/jbc.M301607200;
RA   Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
RT   "Nuclear accumulation of the small GTPase Gsp1p depends on
RT   nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-
RT   CoA carboxylase Acc1p.";
RL   J. Biol. Chem. 278:25331-25340(2003).
RN   [14]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-2; SER-1148 AND SER-1157, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
RA   Mann M., Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone
RT   signaling pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148 AND SER-1157, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-1148; SER-1157
RP   AND SER-1162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1429-2233 IN COMPLEX WITH
RP   COA, CATALYTIC ACTIVITY AS ACETYL-COA CARBOXYLASE, MUTAGENESIS OF
RP   LEU-1705; ARG-1731; TYR-1738; ARG-1954; GLU-1994; GLU-2026 AND
RP   ARG-2036, AND HOMODIMERIZATION.
RX   PubMed=12663926; DOI=10.1126/science.1081366;
RA   Zhang H., Yang Z., Shen Y., Tong L.;
RT   "Crystal structure of the carboxyltransferase domain of acetyl-
RT   coenzyme A carboxylase.";
RL   Science 299:2064-2067(2003).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-566 IN COMPLEX WITH
RP   SORAPHEN, AND SUBUNIT.
RX   PubMed=15610732; DOI=10.1016/j.molcel.2004.11.034;
RA   Shen Y., Volrath S.L., Weatherly S.C., Elich T.D., Tong L.;
RT   "A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A
RT   carboxylase by soraphen A, a macrocyclic polyketide natural product.";
RL   Mol. Cell 16:881-891(2004).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1482-2218 IN COMPLEXES WITH
RP   THE INHIBITORS HALOXYFOP OR DICLOFOP, SUBUNIT, AND CATALYTIC ACTIVITY
RP   AS ACETYL-COA CARBOXYLASE.
RX   PubMed=15079078; DOI=10.1073/pnas.0400891101;
RA   Zhang H., Tweel B., Tong L.;
RT   "Molecular basis for the inhibition of the carboxyltransferase domain
RT   of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5910-5915(2004).
CC   -!- FUNCTION: Carries out three functions: biotin carboxyl carrier
CC       protein, biotin carboxylase and carboxyltransferase. Involved in
CC       the synthesis of very-long-chain fatty acid synthesis which is
CC       required to maintain a functional nuclear envelope. Required for
CC       acylation and vacuolar membrane association of VAC8 which is
CC       necessary to maintain a normal morphology of the vacuole.
CC       {ECO:0000269|PubMed:10757783, ECO:0000269|PubMed:12730220,
CC       ECO:0000269|PubMed:6103540, ECO:0000269|PubMed:6108218,
CC       ECO:0000269|PubMed:8943372}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000269|PubMed:12663926,
CC         ECO:0000269|PubMed:15079078};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWU9};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: By phosphorylation. The catalytic activity is
CC       inhibited by soraphen A, a polyketide isolated from the
CC       myxobacterium Sorangium cellulosum and a potent inhibitor of
CC       fungal growth. {ECO:0000269|PubMed:7916271}.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12663926,
CC       ECO:0000269|PubMed:15079078, ECO:0000269|PubMed:15610732}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-4814, EBI-4814;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Cytoplasmic side.
CC   -!- INDUCTION: Repressed in presence of fatty acids. Repressed 3-fold
CC       by lipid precursors, inositol and choline, and also controlled by
CC       regulatory factors INO2, INO4 and OPI1.
CC       {ECO:0000269|PubMed:1359536, ECO:0000269|PubMed:8098706,
CC       ECO:0000269|PubMed:8127678}.
CC   -!- MISCELLANEOUS: Present with 20200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
DR   EMBL; M92156; AAA20073.1; -; Genomic_DNA.
DR   EMBL; Z71631; CAA96294.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10557.1; -; Genomic_DNA.
DR   PIR; S63347; S63347.
DR   RefSeq; NP_014413.1; NM_001183193.1.
DR   PDB; 1OD2; X-ray; 2.70 A; A/B=1429-2233.
DR   PDB; 1OD4; X-ray; 2.70 A; A/B/C=1429-2233.
DR   PDB; 1UYR; X-ray; 2.50 A; A/B=1482-2218.
DR   PDB; 1UYS; X-ray; 2.80 A; A/B/C=1482-2218.
DR   PDB; 1UYT; X-ray; 2.50 A; A/B/C=1482-2218.
DR   PDB; 1UYV; X-ray; 2.60 A; A/B/C=1482-2218.
DR   PDB; 1W2X; X-ray; 2.80 A; A/B/C=1476-2233.
DR   PDB; 1W93; X-ray; 2.50 A; A=14-566.
DR   PDB; 1W96; X-ray; 1.80 A; A/B/C=13-566.
DR   PDB; 3H0J; X-ray; 2.80 A; A/B/C=1476-2233.
DR   PDB; 3H0Q; X-ray; 2.50 A; A/B/C=1476-2233.
DR   PDB; 3H0S; X-ray; 2.43 A; A/B/C=1476-2233.
DR   PDB; 3K8X; X-ray; 2.30 A; A/B/C=1476-2233.
DR   PDB; 3PGQ; X-ray; 2.80 A; A/B/C=1476-2233.
DR   PDB; 3TV5; X-ray; 2.80 A; A/B/C=1476-2233.
DR   PDB; 3TVU; X-ray; 2.40 A; A/B/C=1476-2233.
DR   PDB; 3TVW; X-ray; 2.80 A; A/B/C=1476-2233.
DR   PDB; 3TZ3; X-ray; 2.70 A; A/B/C=1476-2233.
DR   PDB; 4WYO; X-ray; 2.89 A; B/C=1476-2233.
DR   PDB; 4WZ8; X-ray; 2.23 A; B/C=1476-2233.
DR   PDB; 5CS0; X-ray; 2.50 A; A/B=797-1033.
DR   PDB; 5CS4; X-ray; 3.19 A; A/B=1036-1503.
DR   PDB; 5CSA; X-ray; 3.00 A; A/B=569-1494.
DR   PDB; 5CSK; X-ray; 3.10 A; A/B=22-2233.
DR   PDB; 5CSL; X-ray; 3.20 A; A/B=22-2233.
DR   PDB; 5CTB; X-ray; 2.40 A; A/B/C=1476-2233.
DR   PDB; 5CTC; X-ray; 2.70 A; A/B/C=1476-2233.
DR   PDB; 5CTE; X-ray; 2.34 A; B/C=1476-2233.
DR   PDB; 5I6E; X-ray; 3.00 A; A=768-1494.
DR   PDB; 5TRC; X-ray; 2.90 A; A/B=1036-1503.
DR   PDBsum; 1OD2; -.
DR   PDBsum; 1OD4; -.
DR   PDBsum; 1UYR; -.
DR   PDBsum; 1UYS; -.
DR   PDBsum; 1UYT; -.
DR   PDBsum; 1UYV; -.
DR   PDBsum; 1W2X; -.
DR   PDBsum; 1W93; -.
DR   PDBsum; 1W96; -.
DR   PDBsum; 3H0J; -.
DR   PDBsum; 3H0Q; -.
DR   PDBsum; 3H0S; -.
DR   PDBsum; 3K8X; -.
DR   PDBsum; 3PGQ; -.
DR   PDBsum; 3TV5; -.
DR   PDBsum; 3TVU; -.
DR   PDBsum; 3TVW; -.
DR   PDBsum; 3TZ3; -.
DR   PDBsum; 4WYO; -.
DR   PDBsum; 4WZ8; -.
DR   PDBsum; 5CS0; -.
DR   PDBsum; 5CS4; -.
DR   PDBsum; 5CSA; -.
DR   PDBsum; 5CSK; -.
DR   PDBsum; 5CSL; -.
DR   PDBsum; 5CTB; -.
DR   PDBsum; 5CTC; -.
DR   PDBsum; 5CTE; -.
DR   PDBsum; 5I6E; -.
DR   PDBsum; 5TRC; -.
DR   DisProt; DP00557; -.
DR   ProteinModelPortal; Q00955; -.
DR   SMR; Q00955; -.
DR   BioGrid; 35841; 275.
DR   DIP; DIP-975N; -.
DR   IntAct; Q00955; 42.
DR   MINT; Q00955; -.
DR   STRING; 4932.YNR016C; -.
DR   CarbonylDB; Q00955; -.
DR   iPTMnet; Q00955; -.
DR   MaxQB; Q00955; -.
DR   PaxDb; Q00955; -.
DR   PRIDE; Q00955; -.
DR   EnsemblFungi; YNR016C_mRNA; YNR016C_mRNA; YNR016C.
DR   GeneID; 855750; -.
DR   KEGG; sce:YNR016C; -.
DR   EuPathDB; FungiDB:YNR016C; -.
DR   SGD; S000005299; ACC1.
DR   GeneTree; ENSGT00940000175750; -.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; Q00955; -.
DR   KO; K11262; -.
DR   OMA; LPYGEWN; -.
DR   BioCyc; YEAST:MONOMER3O-7; -.
DR   BRENDA; 6.3.4.14; 984.
DR   BRENDA; 6.4.1.2; 984.
DR   Reactome; R-SCE-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-SCE-196780; Biotin transport and metabolism.
DR   Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-SCE-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   EvolutionaryTrace; Q00955; -.
DR   PRO; PR:Q00955; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IMP:CAFA.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:1905502; F:acetyl-CoA binding; IMP:CAFA.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IMP:SGD.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IMP:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IMP:CAFA.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006998; P:nuclear envelope organization; TAS:SGD.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Biotin; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Membrane;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:15665377,
FT                                ECO:0000244|PubMed:22814378}.
FT   CHAIN         2   2233       Acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000146770.
FT   DOMAIN       58    567       Biotin carboxylation.
FT   DOMAIN      216    408       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      694    768       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1486   1822       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1826   2141       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     256    261       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1486   2141       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   REGION     1627   1629       Acetyl-CoA binding.
FT   ACT_SITE    383    383       {ECO:0000250}.
FT   METAL       365    365       Manganese 1. {ECO:0000250}.
FT   METAL       379    379       Manganese 1. {ECO:0000250}.
FT   METAL       379    379       Manganese 2. {ECO:0000250}.
FT   METAL       381    381       Manganese 2. {ECO:0000250}.
FT   BINDING    1731   1731       Coenzyme A.
FT   BINDING    1998   1998       Acetyl-CoA; via amide nitrogen.
FT   BINDING    2034   2034       Coenzyme A.
FT   BINDING    2036   2036       Coenzyme A.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:15665377,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:15665377}.
FT   MOD_RES     735    735       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   MOD_RES     790    790       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES    1148   1148       Phosphoserine.
FT                                {ECO:0000244|PubMed:15665377,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES    1157   1157       Phosphoserine.
FT                                {ECO:0000244|PubMed:15665377,
FT                                ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES    1162   1162       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN    1705   1705       L->I: Raises KM for malonyl-CoA by a
FT                                factor of 20.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    1731   1731       R->S: Raises KM for malonyl-CoA by a
FT                                factor of 15.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    1738   1738       Y->F: Does not affect catalytic activity.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    1954   1954       R->S: Raises KM for malonyl-CoA by a
FT                                factor of 70.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    1994   1994       E->Q: Does not affect catalytic activity.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    2026   2026       E->Q: Does not affect catalytic activity.
FT                                {ECO:0000269|PubMed:12663926}.
FT   MUTAGEN    2036   2036       R->E: Affects only slightly binding of
FT                                Co-A. {ECO:0000269|PubMed:12663926}.
FT   CONFLICT   1523   1523       W -> G (in Ref. 1; AAA20073).
FT                                {ECO:0000305}.
FT   CONFLICT   1755   1755       I -> IWYRCL (in Ref. 1; AAA20073).
FT                                {ECO:0000305}.
FT   CONFLICT   1761   1766       AINKML -> ESTNA (in Ref. 1; AAA20073).
FT                                {ECO:0000305}.
FT   HELIX        22     27       {ECO:0000244|PDB:1W96}.
FT   HELIX        30     32       {ECO:0000244|PDB:1W96}.
FT   STRAND       35     37       {ECO:0000244|PDB:1W96}.
FT   HELIX        38     40       {ECO:0000244|PDB:1W96}.
FT   HELIX        45     52       {ECO:0000244|PDB:1W96}.
FT   STRAND       61     64       {ECO:0000244|PDB:1W96}.
FT   HELIX        68     86       {ECO:0000244|PDB:1W96}.
FT   STRAND       91     98       {ECO:0000244|PDB:1W96}.
FT   HELIX       100    104       {ECO:0000244|PDB:1W96}.
FT   HELIX       108    112       {ECO:0000244|PDB:1W96}.
FT   STRAND      113    118       {ECO:0000244|PDB:1W96}.
FT   HELIX       124    126       {ECO:0000244|PDB:1W96}.
FT   TURN        127    129       {ECO:0000244|PDB:1W96}.
FT   HELIX       131    140       {ECO:0000244|PDB:1W96}.
FT   STRAND      144    147       {ECO:0000244|PDB:1W96}.
FT   TURN        152    155       {ECO:0000244|PDB:1W96}.
FT   HELIX       158    165       {ECO:0000244|PDB:1W96}.
FT   STRAND      171    174       {ECO:0000244|PDB:1W96}.
FT   HELIX       177    182       {ECO:0000244|PDB:1W96}.
FT   HELIX       186    195       {ECO:0000244|PDB:1W96}.
FT   TURN        204    207       {ECO:0000244|PDB:1W96}.
FT   TURN        215    217       {ECO:0000244|PDB:1W96}.
FT   HELIX       224    227       {ECO:0000244|PDB:1W96}.
FT   HELIX       228    230       {ECO:0000244|PDB:1W96}.
FT   HELIX       235    245       {ECO:0000244|PDB:1W96}.
FT   STRAND      247    253       {ECO:0000244|PDB:1W96}.
FT   TURN        258    261       {ECO:0000244|PDB:1W96}.
FT   STRAND      262    265       {ECO:0000244|PDB:1W96}.
FT   HELIX       268    281       {ECO:0000244|PDB:1W96}.
FT   STRAND      287    291       {ECO:0000244|PDB:1W96}.
FT   STRAND      297    305       {ECO:0000244|PDB:1W96}.
FT   TURN        307    309       {ECO:0000244|PDB:1W93}.
FT   STRAND      311    323       {ECO:0000244|PDB:1W96}.
FT   STRAND      326    333       {ECO:0000244|PDB:1W96}.
FT   HELIX       339    356       {ECO:0000244|PDB:1W96}.
FT   STRAND      360    368       {ECO:0000244|PDB:1W96}.
FT   TURN        370    372       {ECO:0000244|PDB:1W96}.
FT   STRAND      375    381       {ECO:0000244|PDB:1W96}.
FT   HELIX       388    395       {ECO:0000244|PDB:1W96}.
FT   HELIX       399    407       {ECO:0000244|PDB:1W96}.
FT   HELIX       412    414       {ECO:0000244|PDB:1W96}.
FT   HELIX       416    421       {ECO:0000244|PDB:1W96}.
FT   HELIX       439    444       {ECO:0000244|PDB:1W96}.
FT   STRAND      452    462       {ECO:0000244|PDB:1W96}.
FT   STRAND      466    468       {ECO:0000244|PDB:1W93}.
FT   STRAND      472    478       {ECO:0000244|PDB:1W96}.
FT   STRAND      484    492       {ECO:0000244|PDB:1W96}.
FT   STRAND      503    515       {ECO:0000244|PDB:1W96}.
FT   HELIX       516    530       {ECO:0000244|PDB:1W96}.
FT   STRAND      531    536       {ECO:0000244|PDB:5CSK}.
FT   HELIX       541    547       {ECO:0000244|PDB:1W96}.
FT   HELIX       550    553       {ECO:0000244|PDB:1W96}.
FT   HELIX       561    565       {ECO:0000244|PDB:1W96}.
FT   HELIX       577    605       {ECO:0000244|PDB:5CSA}.
FT   HELIX       612    615       {ECO:0000244|PDB:5CSA}.
FT   STRAND      618    624       {ECO:0000244|PDB:5CSA}.
FT   STRAND      626    636       {ECO:0000244|PDB:5CSA}.
FT   STRAND      638    648       {ECO:0000244|PDB:5CSA}.
FT   STRAND      650    657       {ECO:0000244|PDB:5CSA}.
FT   STRAND      659    661       {ECO:0000244|PDB:5CSA}.
FT   STRAND      663    669       {ECO:0000244|PDB:5CSA}.
FT   STRAND      671    675       {ECO:0000244|PDB:5CSA}.
FT   STRAND      682    687       {ECO:0000244|PDB:5CSA}.
FT   STRAND      690    695       {ECO:0000244|PDB:5CSA}.
FT   STRAND      702    704       {ECO:0000244|PDB:5CSA}.
FT   STRAND      709    716       {ECO:0000244|PDB:5CSA}.
FT   STRAND      727    733       {ECO:0000244|PDB:5CSA}.
FT   STRAND      736    741       {ECO:0000244|PDB:5CSA}.
FT   STRAND      746    750       {ECO:0000244|PDB:5CSA}.
FT   STRAND      763    767       {ECO:0000244|PDB:5CSA}.
FT   HELIX       772    774       {ECO:0000244|PDB:5CSA}.
FT   STRAND      793    795       {ECO:0000244|PDB:5I6E}.
FT   HELIX       798    813       {ECO:0000244|PDB:5CS0}.
FT   HELIX       818    833       {ECO:0000244|PDB:5CS0}.
FT   HELIX       838    850       {ECO:0000244|PDB:5CS0}.
FT   HELIX       851    853       {ECO:0000244|PDB:5CS0}.
FT   HELIX       856    871       {ECO:0000244|PDB:5CS0}.
FT   HELIX       878    889       {ECO:0000244|PDB:5CS0}.
FT   TURN        892    894       {ECO:0000244|PDB:5CS0}.
FT   STRAND      896    898       {ECO:0000244|PDB:5CS0}.
FT   HELIX       900    913       {ECO:0000244|PDB:5CS0}.
FT   TURN        914    916       {ECO:0000244|PDB:5CS0}.
FT   HELIX       918    937       {ECO:0000244|PDB:5CS0}.
FT   HELIX       938    940       {ECO:0000244|PDB:5CSA}.
FT   STRAND      942    944       {ECO:0000244|PDB:5CSL}.
FT   HELIX       947    957       {ECO:0000244|PDB:5CSA}.
FT   HELIX       962    972       {ECO:0000244|PDB:5CS0}.
FT   HELIX       975    995       {ECO:0000244|PDB:5CS0}.
FT   HELIX       997   1002       {ECO:0000244|PDB:5CS0}.
FT   HELIX      1004   1011       {ECO:0000244|PDB:5CS0}.
FT   HELIX      1016   1018       {ECO:0000244|PDB:5CS0}.
FT   HELIX      1019   1030       {ECO:0000244|PDB:5CS0}.
FT   HELIX      1037   1052       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1054   1056       {ECO:0000244|PDB:5CSA}.
FT   STRAND     1057   1059       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1062   1066       {ECO:0000244|PDB:5CSA}.
FT   HELIX      1069   1076       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1083   1086       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1087   1090       {ECO:0000244|PDB:5TRC}.
FT   TURN       1095   1097       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1098   1109       {ECO:0000244|PDB:5TRC}.
FT   TURN       1110   1112       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1113   1122       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1124   1134       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1138   1140       {ECO:0000244|PDB:5I6E}.
FT   STRAND     1155   1157       {ECO:0000244|PDB:5CSL}.
FT   HELIX      1158   1160       {ECO:0000244|PDB:5CSL}.
FT   STRAND     1167   1170       {ECO:0000244|PDB:5I6E}.
FT   STRAND     1173   1178       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1183   1185       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1186   1194       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1220   1225       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1235   1255       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1258   1265       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1268   1270       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1274   1279       {ECO:0000244|PDB:5TRC}.
FT   TURN       1280   1283       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1287   1289       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1294   1300       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1303   1305       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1308   1313       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1320   1327       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1334   1342       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1349   1351       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1353   1372       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1378   1380       {ECO:0000244|PDB:5I6E}.
FT   STRAND     1382   1389       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1397   1403       {ECO:0000244|PDB:5TRC}.
FT   TURN       1404   1408       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1409   1411       {ECO:0000244|PDB:5TRC}.
FT   HELIX      1412   1418       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1420   1430       {ECO:0000244|PDB:5TRC}.
FT   TURN       1432   1434       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1437   1445       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1447   1450       {ECO:0000244|PDB:5I6E}.
FT   STRAND     1453   1461       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1463   1465       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1467   1474       {ECO:0000244|PDB:5TRC}.
FT   TURN       1477   1480       {ECO:0000244|PDB:5TRC}.
FT   STRAND     1482   1484       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1490   1493       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1495   1502       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1508   1510       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1511   1526       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1534   1536       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1537   1544       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1546   1548       {ECO:0000244|PDB:1OD2}.
FT   STRAND     1550   1553       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1561   1571       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1580   1587       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1592   1594       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1598   1614       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1618   1622       {ECO:0000244|PDB:4WZ8}.
FT   TURN       1633   1638       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1640   1645       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1649   1651       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1653   1658       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1660   1668       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1672   1674       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1675   1682       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1685   1693       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1696   1698       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1702   1719       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1724   1728       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1735   1742       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1745   1749       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1754   1757       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1759   1766       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1775   1778       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1780   1783       {ECO:0000244|PDB:4WZ8}.
FT   TURN       1784   1787       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1788   1795       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1796   1807       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1812   1816       {ECO:0000244|PDB:5CSK}.
FT   STRAND     1827   1829       {ECO:0000244|PDB:5CTE}.
FT   STRAND     1837   1839       {ECO:0000244|PDB:3K8X}.
FT   HELIX      1843   1848       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1850   1852       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1855   1857       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1867   1870       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1877   1884       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1887   1894       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1899   1903       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1909   1911       {ECO:0000244|PDB:1OD4}.
FT   STRAND     1915   1919       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1926   1940       {ECO:0000244|PDB:4WZ8}.
FT   TURN       1941   1943       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1947   1950       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1953   1956       {ECO:0000244|PDB:5CTE}.
FT   HELIX      1960   1964       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      1967   1979       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1985   1989       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     1994   1996       {ECO:0000244|PDB:3K8X}.
FT   HELIX      1997   2000       {ECO:0000244|PDB:4WZ8}.
FT   TURN       2001   2003       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2005   2008       {ECO:0000244|PDB:4WZ8}.
FT   TURN       2009   2011       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     2012   2017       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     2021   2025       {ECO:0000244|PDB:3K8X}.
FT   HELIX      2027   2034       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2039   2047       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2049   2058       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2059   2063       {ECO:0000244|PDB:5CTB}.
FT   HELIX      2065   2072       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2078   2095       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2100   2106       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     2108   2113       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2115   2117       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2118   2139       {ECO:0000244|PDB:4WZ8}.
FT   STRAND     2142   2144       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2148   2157       {ECO:0000244|PDB:4WZ8}.
FT   HELIX      2168   2186       {ECO:0000244|PDB:4WZ8}.
FT   TURN       2189   2191       {ECO:0000244|PDB:3TVU}.
FT   TURN       2196   2199       {ECO:0000244|PDB:1UYV}.
FT   TURN       2203   2205       {ECO:0000244|PDB:1UYR}.
FT   HELIX      2206   2215       {ECO:0000244|PDB:5CTE}.
FT   HELIX      2223   2233       {ECO:0000244|PDB:5CTE}.
SQ   SEQUENCE   2233 AA;  250353 MW;  0A335AAD9B1F8308 CRC64;
     MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS
     KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP
     GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM
     RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ
     KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE
     VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS
     AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT
     LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF
     RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV
     EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY
     IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD
     GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE
     HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP
     FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY
     SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL
     GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK
     DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK
     VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY
     VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF
     STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH
     QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR
     ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI
     HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS
     DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL
     RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA
     HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN
     AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY
     LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT
     VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV
     RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV
     EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL
     FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP
     GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD
     YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL
     LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS
     SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP
     ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML
     STDDKEKLLK TLK
//
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