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Database: UniProt
Entry: P24182
LinkDB: P24182
Original site: P24182 
ID   ACCC_ECOLI              Reviewed;         449 AA.
AC   P24182; Q2M8V9;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   13-FEB-2019, entry version 184.
DE   RecName: Full=Biotin carboxylase;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A;
DE            Short=ACC;
DE            EC=6.4.1.2;
GN   Name=accC; Synonyms=fabG; OrderedLocusNames=b3256, JW3224;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12;
RX   PubMed=1682920; DOI=10.1073/pnas.88.21.9730;
RA   Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A.,
RA   Tsuru D., Anai M., Sekiguchi M., Tanabe T.;
RT   "Acetyl-CoA carboxylase from Escherichia coli: gene organization and
RT   nucleotide sequence of the biotin carboxylase subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1370469;
RA   Li S.-J., Cronan J.E. Jr.;
RT   "The gene encoding the biotin carboxylase subunit of Escherichia coli
RT   acetyl-CoA carboxylase.";
RL   J. Biol. Chem. 267:855-863(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Best E.A., Knauf V.C.;
RT   "Cloning and characterization of the E. coli fabEG operon encoding
RT   subunits of acetyl-CoA carboxylase.";
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
RX   PubMed=2575489; DOI=10.1089/dna.1989.8.779;
RA   Alix J.-H.;
RT   "A rapid procedure for cloning genes from lambda libraries by
RT   complementation of E. coli defective mutants: application to the fabE
RT   region of the E. coli chromosome.";
RL   DNA 8:779-789(1989).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=7915138; DOI=10.1021/bi00200a004;
RA   Waldrop G.L., Rayment I., Holden H.M.;
RT   "Three-dimensional structure of the biotin carboxylase subunit of
RT   acetyl-CoA carboxylase.";
RL   Biochemistry 33:10249-10256(1994).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
RX   PubMed=10821865; DOI=10.1074/jbc.275.21.16183;
RA   Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.;
RT   "Movement of the biotin carboxylase B-domain as a result of ATP
RT   binding.";
RL   J. Biol. Chem. 275:16183-16190(2000).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP   ARG-19; GLU-23; PHE-363 AND ARG-366.
RX   PubMed=16793549; DOI=10.1016/j.molcel.2006.04.026;
RA   Shen Y., Chou C.-Y., Chang G.-G., Tong L.;
RT   "Is dimerization required for the catalytic activity of bacterial
RT   biotin carboxylase?";
RL   Mol. Cell 22:807-818(2006).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
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   -!- 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   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex.
CC       {ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:16793549}.
CC   -!- INTERACTION:
CC       P0ABD8:accB; NbExp=10; IntAct=EBI-542308, EBI-542320;
CC       P0A9Q5:accD; NbExp=4; IntAct=EBI-542308, EBI-542064;
CC       P16703:cysM; NbExp=3; IntAct=EBI-542308, EBI-542376;
CC       P25539:ribD; NbExp=3; IntAct=EBI-542308, EBI-552457;
DR   EMBL; M79446; AAA23748.1; -; Genomic_DNA.
DR   EMBL; M80458; AAA23409.1; -; Genomic_DNA.
DR   EMBL; M83198; AAA23746.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58059.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76288.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77297.1; -; Genomic_DNA.
DR   EMBL; M32214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JS0632; JS0632.
DR   RefSeq; NP_417722.1; NC_000913.3.
DR   RefSeq; WP_000884639.1; NZ_LN832404.1.
DR   PDB; 1BNC; X-ray; 2.40 A; A/B=1-449.
DR   PDB; 1DV1; X-ray; 1.90 A; A/B=1-449.
DR   PDB; 1DV2; X-ray; 2.50 A; A/B=1-449.
DR   PDB; 1K69; Model; -; A=1-447.
DR   PDB; 2GPS; X-ray; 2.80 A; A/B=1-449.
DR   PDB; 2GPW; X-ray; 2.20 A; A/B/C/D=1-449.
DR   PDB; 2J9G; X-ray; 2.05 A; A/B=1-449.
DR   PDB; 2V58; X-ray; 2.10 A; A/B=1-449.
DR   PDB; 2V59; X-ray; 2.40 A; A/B=1-449.
DR   PDB; 2V5A; X-ray; 2.31 A; A/B=1-449.
DR   PDB; 2VR1; X-ray; 2.60 A; A/B=1-449.
DR   PDB; 2W6M; X-ray; 2.00 A; A/B=1-449.
DR   PDB; 2W6N; X-ray; 1.87 A; A/B=1-449.
DR   PDB; 2W6O; X-ray; 2.50 A; A/C=1-449.
DR   PDB; 2W6P; X-ray; 1.85 A; A/B=1-449.
DR   PDB; 2W6Q; X-ray; 2.05 A; A/B=1-449.
DR   PDB; 2W6Z; X-ray; 1.90 A; A/B=1-449.
DR   PDB; 2W70; X-ray; 1.77 A; A/B=1-449.
DR   PDB; 2W71; X-ray; 1.99 A; A/C=1-449.
DR   PDB; 3G8C; X-ray; 2.00 A; A/B=1-444.
DR   PDB; 3G8D; X-ray; 1.90 A; A/B=1-444.
DR   PDB; 3JZF; X-ray; 2.13 A; A/B=1-449.
DR   PDB; 3JZI; X-ray; 2.31 A; A/B=1-449.
DR   PDB; 3RUP; X-ray; 1.99 A; A/B=1-449.
DR   PDB; 3RV3; X-ray; 1.91 A; A/B=1-449.
DR   PDB; 3RV4; X-ray; 1.98 A; A=1-449.
DR   PDB; 4HR7; X-ray; 2.50 A; A/C/E/F=1-449.
DR   PDBsum; 1BNC; -.
DR   PDBsum; 1DV1; -.
DR   PDBsum; 1DV2; -.
DR   PDBsum; 1K69; -.
DR   PDBsum; 2GPS; -.
DR   PDBsum; 2GPW; -.
DR   PDBsum; 2J9G; -.
DR   PDBsum; 2V58; -.
DR   PDBsum; 2V59; -.
DR   PDBsum; 2V5A; -.
DR   PDBsum; 2VR1; -.
DR   PDBsum; 2W6M; -.
DR   PDBsum; 2W6N; -.
DR   PDBsum; 2W6O; -.
DR   PDBsum; 2W6P; -.
DR   PDBsum; 2W6Q; -.
DR   PDBsum; 2W6Z; -.
DR   PDBsum; 2W70; -.
DR   PDBsum; 2W71; -.
DR   PDBsum; 3G8C; -.
DR   PDBsum; 3G8D; -.
DR   PDBsum; 3JZF; -.
DR   PDBsum; 3JZI; -.
DR   PDBsum; 3RUP; -.
DR   PDBsum; 3RV3; -.
DR   PDBsum; 3RV4; -.
DR   PDBsum; 4HR7; -.
DR   ProteinModelPortal; P24182; -.
DR   SMR; P24182; -.
DR   BioGrid; 4262456; 269.
DR   ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DR   DIP; DIP-9035N; -.
DR   IntAct; P24182; 20.
DR   STRING; 316385.ECDH10B_3431; -.
DR   BindingDB; P24182; -.
DR   DrugBank; DB08074; 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine.
DR   EPD; P24182; -.
DR   jPOST; P24182; -.
DR   PaxDb; P24182; -.
DR   PRIDE; P24182; -.
DR   EnsemblBacteria; AAC76288; AAC76288; b3256.
DR   EnsemblBacteria; BAE77297; BAE77297; BAE77297.
DR   GeneID; 947761; -.
DR   KEGG; ecj:JW3224; -.
DR   KEGG; eco:b3256; -.
DR   PATRIC; fig|511145.12.peg.3355; -.
DR   EchoBASE; EB0272; -.
DR   EcoGene; EG10276; accC.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   InParanoid; P24182; -.
DR   KO; K01961; -.
DR   PhylomeDB; P24182; -.
DR   BioCyc; EcoCyc:BIOTIN-CARBOXYL-MONOMER; -.
DR   BioCyc; ECOL316407:JW3224-MONOMER; -.
DR   BioCyc; MetaCyc:BIOTIN-CARBOXYL-MONOMER; -.
DR   BRENDA; 6.3.4.14; 2026.
DR   SABIO-RK; P24182; -.
DR   UniPathway; UPA00655; UER00711.
DR   EvolutionaryTrace; P24182; -.
DR   PRO; PR:P24182; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IDA:EcoliWiki.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:EcoliWiki.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00514; accC; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Biotin; Complete proteome;
KW   Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    449       Biotin carboxylase.
FT                                /FTId=PRO_0000146791.
FT   DOMAIN        1    445       Biotin carboxylation.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    292    292       {ECO:0000255}.
FT   BINDING     116    116       ATP. {ECO:0000269|PubMed:10821865}.
FT   BINDING     201    201       ATP. {ECO:0000269|PubMed:10821865}.
FT   BINDING     236    236       ATP. {ECO:0000269|PubMed:10821865}.
FT   MUTAGEN      19     19       R->E: Loss of homodimerization. No effect
FT                                on ATP binding.
FT                                {ECO:0000269|PubMed:16793549}.
FT   MUTAGEN      23     23       E->R: Loss of homodimerization. No effect
FT                                on ATP binding.
FT                                {ECO:0000269|PubMed:16793549}.
FT   MUTAGEN     363    363       F->A: Loss of homodimerization. No effect
FT                                on ATP binding.
FT                                {ECO:0000269|PubMed:16793549}.
FT   MUTAGEN     366    366       R->E: Loss of homodimerization. No effect
FT                                on ATP binding.
FT                                {ECO:0000269|PubMed:16793549}.
FT   CONFLICT    136    136       G -> A (in Ref. 7). {ECO:0000305}.
FT   CONFLICT    160    160       A -> P (in Ref. 7). {ECO:0000305}.
FT   CONFLICT    260    261       CA -> SR (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    313    313       L -> M (in Ref. 1; AAA23748).
FT                                {ECO:0000305}.
FT   STRAND        3      7       {ECO:0000244|PDB:2W70}.
FT   HELIX        11     24       {ECO:0000244|PDB:2W70}.
FT   STRAND       27     33       {ECO:0000244|PDB:2W70}.
FT   HELIX        34     36       {ECO:0000244|PDB:2W70}.
FT   HELIX        40     44       {ECO:0000244|PDB:2W70}.
FT   STRAND       45     52       {ECO:0000244|PDB:2W70}.
FT   HELIX        56     58       {ECO:0000244|PDB:2W70}.
FT   TURN         59     61       {ECO:0000244|PDB:2W70}.
FT   HELIX        63     73       {ECO:0000244|PDB:2W70}.
FT   STRAND       77     79       {ECO:0000244|PDB:2W70}.
FT   TURN         84     87       {ECO:0000244|PDB:2W70}.
FT   HELIX        89     97       {ECO:0000244|PDB:2W70}.
FT   STRAND      101    105       {ECO:0000244|PDB:2W70}.
FT   HELIX       107    114       {ECO:0000244|PDB:2W70}.
FT   HELIX       116    126       {ECO:0000244|PDB:2W70}.
FT   HELIX       142    152       {ECO:0000244|PDB:2W70}.
FT   STRAND      154    160       {ECO:0000244|PDB:2W70}.
FT   TURN        165    168       {ECO:0000244|PDB:2W70}.
FT   STRAND      170    172       {ECO:0000244|PDB:2W70}.
FT   HELIX       175    193       {ECO:0000244|PDB:2W70}.
FT   STRAND      198    202       {ECO:0000244|PDB:2W70}.
FT   STRAND      208    216       {ECO:0000244|PDB:2W70}.
FT   STRAND      218    220       {ECO:0000244|PDB:2W6O}.
FT   STRAND      222    234       {ECO:0000244|PDB:2W70}.
FT   STRAND      237    244       {ECO:0000244|PDB:2W70}.
FT   HELIX       250    267       {ECO:0000244|PDB:2W70}.
FT   STRAND      271    280       {ECO:0000244|PDB:2W70}.
FT   STRAND      283    290       {ECO:0000244|PDB:2W70}.
FT   HELIX       297    304       {ECO:0000244|PDB:2W70}.
FT   HELIX       308    317       {ECO:0000244|PDB:2W70}.
FT   HELIX       325    327       {ECO:0000244|PDB:2W70}.
FT   STRAND      332    340       {ECO:0000244|PDB:2W70}.
FT   TURN        344    346       {ECO:0000244|PDB:2W70}.
FT   STRAND      356    358       {ECO:0000244|PDB:2W70}.
FT   STRAND      365    368       {ECO:0000244|PDB:2W70}.
FT   STRAND      379    381       {ECO:0000244|PDB:2W70}.
FT   STRAND      383    394       {ECO:0000244|PDB:2W70}.
FT   HELIX       395    408       {ECO:0000244|PDB:2W70}.
FT   STRAND      410    414       {ECO:0000244|PDB:2W70}.
FT   HELIX       418    425       {ECO:0000244|PDB:2W70}.
FT   HELIX       428    432       {ECO:0000244|PDB:2W70}.
FT   HELIX       439    444       {ECO:0000244|PDB:2W70}.
SQ   SEQUENCE   449 AA;  49321 MW;  68C55F10ACB4F170 CRC64;
     MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY
     LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI
     AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ
     SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV
     EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT
     EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP
     GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL
     QIRIMNDENF QHGGTNIHYL EKKLGLQEK
//
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