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Database: UniProt
Entry: A0A1S9IGK2_9CLOT
LinkDB: A0A1S9IGK2_9CLOT
Original site: A0A1S9IGK2_9CLOT 
ID   A0A1S9IGK2_9CLOT        Unreviewed;       448 AA.
AC   A0A1S9IGK2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
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   ORFNames=BS638_02700 {ECO:0000313|EMBL:OOO69459.1};
OS   Clostridium tepidum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO69459.1, ECO:0000313|Proteomes:UP000190256};
RN   [1] {ECO:0000313|EMBL:OOO69459.1, ECO:0000313|Proteomes:UP000190256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO69459.1,
RC   ECO:0000313|Proteomes:UP000190256};
RA   Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA   Samadpour M.;
RT   "Clostridium tepidum sp. nov., a close relative of Clostridium
RT   sporogenes and Clostridium botulinum Group I.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOO69459.1}.
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DR   EMBL; MRAE01000004; OOO69459.1; -; Genomic_DNA.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000190256; Unassembled WGS sequence.
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:UP000190256};
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}.
FT   DOMAIN        1    446       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   448 AA;  49661 MW;  FD998C042AC4618A CRC64;
     MFKKILVANR GEIAVRIIRA CREMGIETVA IYSEADKEAL HVQLADEAVC IGPPSSKDSY
     LNMYNIISAT VLTGSQAIHP GFGFLSENSK FANMCKDCNI VFIGPDSDTI DKMGNKSNAR
     DVMIKAGVPV IPGSNGVIKD EKEALNIAEK IGYPVVVKAS AGGGGRGIRI VHSKENMIKA
     FNAARSEAEG AFGDDSMYIE KFIKNPRHIE FQILGDNYGN IVHLGERDCS LQRRNQKVLE
     EAPSPSMNEE LRKKMGDAAI KAAKAVGYKN AGTIEFLLDE DGSFYFMEMN TRIQVEHPIT
     EMVTGIDILK EQIKIAYGEK LNVAQEDIKI QGHAIECRIN AEDYKNGFRP CPGTIENLYT
     PGGLGVRLDS SVYSGYTIPP YYDSMIGKLI AYGRDREEAI QIMKRALGEF IIEGVNTNID
     FQFIILEDEN FIKGKYTTKY IEKMLTDN
//
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