ID ACCC_ANASP Reviewed; 447 AA. AC Q06862; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 16-JUN-2009, entry version 70. 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; OrderedLocusNames=alr0939; OS Anabaena sp. (strain PCC 7120). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93352435; PubMed=8102363; RA Gornicki P., Scappino L.A., Haselkorn R.; RT "Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena RT sp. strain PCC 7120: biotin carboxylase and biotin carboxyl carrier RT protein."; RL J. Bacteriol. 175:5268-5272(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., RA 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + biotin-carboxyl-carrier protein + CO(2) CC = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. CC -!- SUBUNIT: Acetyl-CoA carboxylase is an heterohexamer of biotin CC carboxyl carrier protein, biotin carboxylase and the two subunits CC of carboxyl transferase in a 2:2 complex (By similarity). CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC -!- SIMILARITY: Contains 1 biotin carboxylation domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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; NP_484982.1; -. DR HSSP; P24182; 1BNC. DR GeneID; 1104533; -. DR GenomeReviews; BA000019_GR; alr0939. DR KEGG; ana:alr0939; -. DR NMPDR; fig|103690.1.peg.1249; -. DR HOGENOM; Q06862; -. DR OMA; Q06862; HIRLMGD. DR BioCyc; NSP103690:ALR0939-MON; -. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009374; F:biotin binding; IEA:InterPro. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR011764; BC. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd. DR InterPro; IPR005481; CarbamoylP_synth_lsu_N. DR InterPro; IPR013817; Pre-ATP_grasp. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; CPSase_L_chain; 1. DR Pfam; PF02786; CPSase_L_D2; 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 3: Inferred from homology; KW ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis; KW Ligase; Lipid synthesis; Nucleotide-binding. FT CHAIN 1 447 Biotin carboxylase. FT /FTId=PRO_0000146787. FT DOMAIN 1 447 Biotin carboxylation. FT DOMAIN 121 318 ATP-grasp. FT ACT_SITE 293 293 By similarity. FT BINDING 117 117 ATP (By similarity). FT BINDING 201 201 ATP (By similarity). FT BINDING 236 236 ATP (By similarity). 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 //