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Entry: A0A1J0WHQ3_9RHOB
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ID   A0A1J0WHQ3_9RHOB        Unreviewed;       450 AA.
AC   A0A1J0WHQ3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 13.
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=BOO69_10840 {ECO:0000313|EMBL:APE43855.1};
OS   Sulfitobacter sp. AM1-D1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE43855.1, ECO:0000313|Proteomes:UP000181897};
RN   [1] {ECO:0000313|EMBL:APE43855.1, ECO:0000313|Proteomes:UP000181897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM1-D1 {ECO:0000313|EMBL:APE43855.1,
RC   ECO:0000313|Proteomes:UP000181897};
RA   Yang Q., Zhang X., Tian X.;
RT   "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic
RT   bacteria associated with marine dinoflagellate Alexandrium minutum in
RT   East China Sea.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP018076; APE43855.1; -; Genomic_DNA.
DR   RefSeq; WP_071972192.1; NZ_CP018076.1.
DR   KEGG; suam:BOO69_10840; -.
DR   KO; K01961; -.
DR   OrthoDB; 361205at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000181897; 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:UP000181897};
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:UP000181897}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   450 AA;  49150 MW;  EB41648B6A4EB0BE CRC64;
     MFSKILVANR GEIALRVIRA AREMGIQSVA VHSTADSDAM HVRMADESVC IGPPSSTQSY
     LSIPSIIAAC EITGAEAIHP GYGFLSENAG FVQVVEDHGL TFIGPTAEHI RIMGDKITAK
     ETMRKLGVPC VPGSEGGVAS LEEAKRLGEE IGYPVIIKAT AGGGGKGMKV ATSVADMERA
     FQTARAEGKS NFGNDEVYIE KYLTTPRHIE IQVFGDGKGR AVHLGERDCS LQRRHQKVFE
     EAPGPAISEE ERARIGKTCA DAMADINYIG AGTIEFLYEN GEFYFIEMNT RLQVEHPVTE
     GIFGVDLVRE QIQVASGMPM SFRQEDLKIN GHAIEVRLNA EKLPNFRPSP GRISQYHAPG
     GLGVRMDSAI YDGYSIPPYY DSLIGKLIVQ GRDRPEALAR LGRALGELII DGIDTTVPLF
     HALLREKDIQ TGDYNIHWLE HWLETNLGDG
//
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