ID ACCC_NOSS1 Reviewed; 447 AA. AC Q06862; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 141. 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=alr0939; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8102363; DOI=10.1128/jb.175.16.5268-5272.1993; RA Gornicki P., Scappino L.A., Haselkorn R.; RT "Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp. RT strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein."; RL J. Bacteriol. 175:5268-5272(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(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; L14862; AAB51770.1; -; Genomic_DNA. DR EMBL; BA000019; BAB72896.1; -; Genomic_DNA. DR PIR; A53311; A53311. DR PIR; AH1923; AH1923. DR RefSeq; WP_010995113.1; NZ_RSCN01000006.1. DR AlphaFoldDB; Q06862; -. DR SMR; Q06862; -. DR STRING; 103690.gene:10492953; -. DR KEGG; ana:alr0939; -. DR eggNOG; COG0439; Bacteria. DR OrthoDB; 9807469at2; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000002483; 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; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. 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..447 FT /note="Biotin carboxylase" FT /id="PRO_0000146787" FT DOMAIN 1..447 FT /note="Biotin carboxylation" FT DOMAIN 121..318 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 293 FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 117 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 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 289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 289 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 289 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 289 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 289 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 291 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 293 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 296 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 339 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 339 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" SQ SEQUENCE 447 AA; 49104 MW; 8A541B38B39E00F9 CRC64; MKFDKILIAN RGEIALRILR ACEEMGIATI AVHSTVDRNA LHVQLADEAV CIGEPASAKS YLNIPNIIAA ALTRNASAIH PGYGFLSENA KFAEICADHH IAFIGPTPEA IRLMGDKSTA KETMQKAGVP TVPGSEGLVE TEQEGLELAK DIGYPVMIKA TAGGGGRGMR LVRSPDEFVK LFLAAQGEAG AAFGNAGVYI EKFIERPRHI EFQILADNYG NVIHLGERDC SIQRRNQKLL EEAPSPALDS DLREKMGQAA VKAAQFINYT GAGTIEFLLD RSGQFYFMEM NTRIQVEHPV TEMVTGVDLL VEQIRIAQGE RLRLTQDQVV LRGHAIECRI NAEDPDHDFR PAPGRISGYL PPGGPGVRID SHVYTDYQIP PYYDSLIGKL IVWGPDRATA INRMKRALRE CAITGLPTTI GFHQRIMENP QFLQGNVSTS FVQEMNK //