ID ACCC_ECO57 Reviewed; 449 AA. AC Q8X9B6; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14 {ECO:0000250|UniProtKB:P24182}; DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305}; GN Name=accC; OrderedLocusNames=Z4616, ECs4128; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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 {ECO:0000250|UniProtKB:P24182}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, CC ChEBI:CHEBI:456216; EC=6.3.4.14; CC Evidence={ECO:0000250|UniProtKB:P24182}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00409}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P24182}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl CC carrier protein, biotin carboxylase and the two subunits of carboxyl CC transferase in a 2:2 complex. {ECO:0000250|UniProtKB:P24182}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005174; AAG58384.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37551.1; -; Genomic_DNA. DR PIR; D85990; D85990. DR PIR; H91144; H91144. DR RefSeq; NP_312155.1; NC_002695.1. DR RefSeq; WP_000884642.1; NZ_VOAI01000014.1. DR AlphaFoldDB; Q8X9B6; -. DR SMR; Q8X9B6; -. DR STRING; 155864.Z4616; -. DR GeneID; 916024; -. DR KEGG; ece:Z4616; -. DR KEGG; ecs:ECs_4128; -. DR PATRIC; fig|386585.9.peg.4311; -. DR eggNOG; COG0439; Bacteria. DR HOGENOM; CLU_000395_3_2_6; -. DR OMA; FINKPKH; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; Chromosome. 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; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. 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 NCBIfam; TIGR00514; accC; 1. DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1. 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 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 3: Inferred from homology; KW ATP-binding; Biotin; Fatty acid biosynthesis; Fatty acid metabolism; KW Ligase; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..449 FT /note="Biotin carboxylase" FT /id="PRO_0000146792" FT DOMAIN 1..445 FT /note="Biotin carboxylation" FT DOMAIN 120..317 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 292 FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 159 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 165..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 201..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 238 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 276 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 276 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 290 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 292 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 295 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 338 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 338 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" SQ SEQUENCE 449 AA; 49337 MW; BC5716323F6233ED CRC64; MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NSIYLAERDC SMQRRHQKVV EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK //