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Entry: Q06862
LinkDB: Q06862
Original site: Q06862 
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   13-NOV-2013, entry version 101.
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; IRRMQNA; -.
DR   OrthoDB; EOG6CVV6Z; -.
DR   ProtClustDB; PRK08591; -.
DR   UniPathway; UPA00655; UER00711.
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: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; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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
//
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