ID ACCC_ALLVD Reviewed; 449 AA. AC O52058; D3RUH1; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 27-MAR-2024, entry version 120. DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14 {ECO:0000250|UniProtKB:O04983}; DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305}; GN Name=accC; OrderedLocusNames=Alvin_1906; OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB OS 10441 / D) (Chromatium vinosum). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Allochromatium. OX NCBI_TaxID=572477; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D; RX PubMed=22675582; DOI=10.4056/sigs.2335270; RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C., RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.; RT "Complete genome sequence of Allochromatium vinosum DSM 180(T)."; RL Stand. Genomic Sci. 5:311-330(2011). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-449. RX PubMed=9560425; DOI=10.1007/s002030050594; RA Pattaragulwanit K., Brune D.C., Trueper H.G., Dahl C.; RT "Molecular genetic evidence for extracytoplasmic localization of sulfur RT globules in Chromatium vinosum."; RL Arch. Microbiol. 169:434-444(1998). 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:O04983}. 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:O04983}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00969}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00969}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00969}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. 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}. 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; CP001896; ADC62830.1; -; Genomic_DNA. DR EMBL; AF017119; AAB91545.1; -; Genomic_DNA. DR AlphaFoldDB; O52058; -. DR SMR; O52058; -. DR STRING; 572477.Alvin_1906; -. DR KEGG; alv:Alvin_1906; -. DR eggNOG; COG0439; Bacteria. DR HOGENOM; CLU_000395_3_2_6; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000001441; 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; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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 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_0000146790" FT DOMAIN 4..448 FT /note="Biotin carboxylation" FT DOMAIN 123..320 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 295 FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 168..169 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 204..207 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 241 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 279 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 291 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 291 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 291 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 293 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 295 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 298 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 341 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 341 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT CONFLICT 427 FT /note="I -> L (in Ref. 2; AAB91545)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="Missing (in Ref. 2; AAB91545)" FT /evidence="ECO:0000305" SQ SEQUENCE 449 AA; 49268 MW; 40510894E20C82E4 CRC64; MSAMIEKVLI ANRGEIALRI LRACRELGIK TVAVHSEADR DLKHVLLADE SVCIGPAPAM QSYLNVPAII SAAEVTDTVA IHPGYGFLSE NADFAERVEK SGFIFIGPRP ETIRLMGDKV SAIAAMKAAG VPCVPGSDGP IDDNKKRTLE LAREIGYPIM IKSSGGGGGR GMRVVHSEAT LLNAIALTRA EAAAAFNNDM VYMEKYLENP RHIEFQVLAD QMGNAIHLGE RDCSMQRRHQ KVVEEAPAPG ITEEQRREIG ERCAAACRSI GYRGAGTFEF LYENGQFYFI EMNTRVQVEH PVTEMVTGVD IVKEQILIAA GEPLRYRQSD IQMRGHAIEC RINAEHPETF MPSPGKITDF HAPGGPGVRI ETHIYSGYTV PCHYDSMIGK LITHGEDRES AVARMCNALR ETVIEGIHSN IKLQRSIMRD GAFLAGGANI HYLEKMLGL //