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Database: UniProt
Entry: D7DVJ3_NOSA0
LinkDB: D7DVJ3_NOSA0
Original site: D7DVJ3_NOSA0 
ID   D7DVJ3_NOSA0            Unreviewed;       448 AA.
AC   D7DVJ3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE            EC=6.4.1.2 {ECO:0000256|RuleBase:RU365063};
GN   OrderedLocusNames=Aazo_0051 {ECO:0000313|EMBL:ADI62705.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI62705.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI62705.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI62705.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted
RT   endosymbiotic multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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:0000256|RuleBase:RU365063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|RuleBase:RU365063}.
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.
CC       {ECO:0000256|RuleBase:RU365063}.
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DR   EMBL; CP002059; ADI62705.1; -; Genomic_DNA.
DR   RefSeq; WP_013189725.1; NC_014248.1.
DR   STRING; 551115.Aazo_0051; -.
DR   EnsemblBacteria; ADI62705; ADI62705; Aazo_0051.
DR   KEGG; naz:Aazo_0051; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 361205at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001511; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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   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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Biotin {ECO:0000256|RuleBase:RU365063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001511};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511}.
FT   DOMAIN        2    447       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    318       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   448 AA;  49289 MW;  D67C22E2EC496684 CRC64;
     MKFDKILIAN RGEIALRILR ACEEMGIATV AIHSTVDRNA LHVQLADEAV CIGEPASSKS
     YLNIPNIIAA ALTRGATAIH PGYGFLAENA RFAEICADHQ IVFIGPTPEA IRLMGDKSTA
     KETMQKAGVP TVPGSDGLVE SDQEGKLIAK DIGYPVMIKA TAGGGGRGMR LVLSEDEFVK
     LFLAAQGEAG AAFGNAGVYI EKSIERPRHI EFQILADSYG NVIHLGERDC SIQRRNQKLL
     EEAPSPALDE ELRERMGQAA VKAARFINYT GAGTIEFLLD KSGKFYFMEM NTRIQVEHPV
     TEMVTGIDLL VEQIRIAQGE RLQLTQEQVI LRGHAIECRI NAEDPEHDFR PSPGKISGYL
     PPGGPGVRID SHVYTDYQIP PYYDSLIGKL IVWGPDRSTA INRMKRALRE CAITGLPTTI
     GFHQKIMETP QFLQGNVYTN FVQEMKEQ
//
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