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Database: UniProt
Entry: P32874
LinkDB: P32874
Original site: P32874 
ID   HFA1_YEAST              Reviewed;        2273 AA.
AC   P32874; D6W032; O42823;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   13-FEB-2019, entry version 173.
DE   RecName: Full=Acetyl-CoA carboxylase, mitochondrial;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
DE   Flags: Precursor;
GN   Name=HFA1; OrderedLocusNames=YMR207C; ORFNames=YM8261.01C, YM8325.08C;
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].
RC   STRAIN=SP1;
RA   Saito A., Kazuta Y., Kondo H., Tanabe T.;
RT   "Occurrence of an acetyl-CoA carboxylase-like gene in Saccharomyces
RT   serevisiae.";
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-949.
RX   PubMed=7906156; DOI=10.3109/10425179309015625;
RA   Kearsey S.E.;
RT   "Identification of a Saccharomyces cerevisiae gene closely related to
RT   FAS3 (acetyl-CoA carboxylase).";
RL   DNA Seq. 4:69-70(1993).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
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   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14761959; DOI=10.1074/jbc.M401071200;
RA   Hoja U., Marthol S., Hofmann J., Stegner S., Schulz R., Meier S.,
RA   Greiner E., Schweizer E.;
RT   "HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls
RT   mitochondrial fatty acid synthesis in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 279:21779-21786(2004).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the
CC       mitochondrial fatty acid synthesis (FAS) type II pathway.
CC       Responsible for the production of the mitochondrial malonyl-CoA,
CC       used for the biosynthesis of the cofactor lipoic acid. This
CC       protein carries three functions: biotin carboxyl carrier protein,
CC       biotin carboxylase, and carboxyltransferase.
CC       {ECO:0000269|PubMed:14761959}.
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   -!- 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   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14761959}.
CC   -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- CAUTION: The reading frame from which this protein is translated
CC       has no Met initiation codon near to the 5'-end. However, it is not
CC       a pseudogene. It has been shown (PubMed:14761959) that at least 72
CC       residues upstream of the first in-frame start codon (Met-151) are
CC       required for function and proper subcellular location. May be
CC       translated by means of alternative initiation codon usage,
CC       programmed translational frame shifting, or mRNA editing.
CC       {ECO:0000305|PubMed:14761959}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DAA10106.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; D78165; BAA24410.1; -; Genomic_DNA.
DR   EMBL; Z49809; CAA89922.1; -; Genomic_DNA.
DR   EMBL; Z48755; CAA88647.1; -; Genomic_DNA.
DR   EMBL; Z22558; CAA80280.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10106.1; ALT_INIT; Genomic_DNA.
DR   PIR; S55089; S55089.
DR   RefSeq; NP_013934.1; NM_001182714.1.
DR   ProteinModelPortal; P32874; -.
DR   SMR; P32874; -.
DR   BioGrid; 35385; 254.
DR   DIP; DIP-2568N; -.
DR   IntAct; P32874; 2.
DR   MINT; P32874; -.
DR   STRING; 4932.YMR207C; -.
DR   MaxQB; P32874; -.
DR   PaxDb; P32874; -.
DR   PeptideAtlas; P32874; -.
DR   PRIDE; P32874; -.
DR   GeneID; 855247; -.
DR   KEGG; sce:YMR207C; -.
DR   EuPathDB; FungiDB:YMR207C; -.
DR   SGD; S000004820; HFA1.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; P32874; -.
DR   KO; K11262; -.
DR   BioCyc; MetaCyc:YMR207C-MONOMER; -.
DR   BioCyc; YEAST:YMR207C-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:P32874; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IGI:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IGI:SGD.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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   ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1    104       Mitochondrion. {ECO:0000255}.
FT   CHAIN       105   2273       Acetyl-CoA carboxylase, mitochondrial.
FT                                /FTId=PRO_0000146771.
FT   DOMAIN      134    635       Biotin carboxylation.
FT   DOMAIN      292    484       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      763    837       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1532   1867       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1871   2187       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     332    337       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1532   2187       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    459    459       {ECO:0000250}.
FT   BINDING    1776   1776       Coenzyme A. {ECO:0000250}.
FT   BINDING    2080   2080       Coenzyme A. {ECO:0000250}.
FT   BINDING    2082   2082       Coenzyme A. {ECO:0000250}.
FT   MOD_RES     804    804       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT    661    661       F -> L (in Ref. 4; CAA80280).
FT                                {ECO:0000305}.
FT   CONFLICT   1027   1027       K -> E (in Ref. 1; BAA24410).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2273 AA;  259163 MW;  08727A301549DA92 CRC64;
     KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT GSQIVRLKGQ
     RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK HTRLPPQFIG LNTVESAQPS
     ILRDFVDLRG GHTVISKILI ANNGIAAVKE MRSIRKWAYE TFNDEKIIQF VVMATPDDLH
     ANSEYIRMAD QYVQVPGGTN NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA
     SSQRKILFIG PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD
     DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL YRQAVNETPG
     SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR HQKIIEEAPV TITKPETFQR
     MERAAIRLGE LVGYVSAGTV EYLYSPKDDK FYFLELNPRL QVEHPTTEMI SGVNLPATQL
     QIAMGIPMHM ISDIRKLYGL DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST
     GKIHELNFRS SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI
     RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI ICGAAMKAYV
     FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL FNVAQSSEEQ FILSINKSQC
     EVNVQKLSSD CLLISVDGKC HTVYWKDDIR GTRLSIDSNT IFLEAELNPT QVISPTPGKL
     VKYLVRSGDH VFAGQQYAEI EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS
     PSKANESSLY RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK
     ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM KRYLEENTND
     HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE KIFENHDIHE ERNLLNLRRK
     DLTNLKKILC ISLSHANVVA KNKLVTAILH EYEPLCQDSS KMSLKFRAVI HDLASLESKW
     AKEVAVKARS VLLRGIFPPI KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH
     SNLIQLQDLF FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
     NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER
     LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPAVK
     FYSFDGTTYD EISQIRNMDP SYEAPLELGK MSNYKIRSLP TYDSSIRIFE GISKFTPLDK
     RFFVRKIINS FMYNDQKTTE ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN
     IPVHRLEEIV STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI
     ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG TTYVYDFPGL
     FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR EPGLNNIGMV AFEIMVQTPE
     YPEGRNMIVI SNDITYNIGS FGPREDLFFD RVTNYARERG IPRIYLAANS GAKLGIAEEL
     IPLFRVAWND PSDPTKGFQY LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG
     FEEGLGVECL QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
     LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT WLSYVPAKRD
     MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN NFQSGLFDKD SFFETLSGWA
     KGVIVGRARL GGIPVGVIAV ETKTIEEIIP ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ
     TINDFNYGEQ LPLIILANWR GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE
     LRGGSWVVID PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL
     RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML VKGVIRNELE
     WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD LLKIVQSWYN DLDVNDDRAV
     VEFIERNSKK IDKNIEEFEI SLLIDELKKK FEDRRGNIVL EELTRLVDSK RKR
//
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