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 01-MAY-2013, entry version 99.
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 Nostoc sp. (strain PCC 7120 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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].
RC STRAIN=PCC 7120 / UTEX 2576;
RX 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] +
CC CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
CC 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 a 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.
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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; NC_003272.1.
DR ProteinModelPortal; Q06862; -.
DR SMR; Q06862; 3-444.
DR STRING; 103690.alr0939; -.
DR EnsemblBacteria; BAB72896; BAB72896; BAB72896.
DR GeneID; 1104533; -.
DR KEGG; ana:alr0939; -.
DR PATRIC; 22771750; VBINosSp37423_1359.
DR eggNOG; COG0439; -.
DR HOGENOM; HOG000008988; -.
DR KO; K01961; -.
DR OMA; ECAITGL; -.
DR ProtClustDB; PRK08591; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; CPSase_L_chain; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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 Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW 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
//
