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Entry: A0A1B1FQP6_9BACT
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ID   A0A1B1FQP6_9BACT        Unreviewed;       447 AA.
AC   A0A1B1FQP6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-FEB-2019, entry version 14.
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=MY04_1084 {ECO:0000313|EMBL:ANQ48461.1};
OS   Flammeovirga sp. MY04.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=1191459 {ECO:0000313|EMBL:ANQ48461.1, ECO:0000313|Proteomes:UP000092715};
RN   [1] {ECO:0000313|EMBL:ANQ48461.1, ECO:0000313|Proteomes:UP000092715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MY04 {ECO:0000313|EMBL:ANQ48461.1,
RC   ECO:0000313|Proteomes:UP000092715};
RA   Han W., Gu J., Liu H., Li Z., Han K., Li Y.;
RT   "The genome sequence and the agarase system of a polysaccharide-
RT   degrading marine bacterium, Flammeovirga sp. MY04.";
RL   Submitted (MAY-2012) 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; CP003560; ANQ48461.1; -; Genomic_DNA.
DR   RefSeq; WP_066207424.1; NZ_CP003560.1.
DR   EnsemblBacteria; ANQ48461; ANQ48461; MY04_1084.
DR   KEGG; flm:MY04_1084; -.
DR   PATRIC; fig|1191459.5.peg.1090; -.
DR   KO; K01961; -.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; GCF_001682195:G1EXC-1081-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000092715; Chromosome 1.
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:UP000092715};
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:UP000092715}.
FT   DOMAIN        1    444       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   447 AA;  49069 MW;  2604D03BA2B500E0 CRC64;
     MFKKILIANR GEIALRVIRT CSEMGIKTVA VYSTADKESL HVKFADEAVC IGPAASTDSY
     LNIPNILAAA EITNCDAIHP GYGFLSENAN FSRICEENNI KFIGASADMI DSMGDKATAK
     ATMKEAGVPT IPGSEGLLDS VEQGLEIAEQ IKYPVILKAT AGGGGRGMRI VTSPDEFQKA
     WDSARQESAA AFGNDGMYLE KFVEEPRHVE IQIIGDSYGS ACHLSERDCS IQRRHQKLTE
     EAPSPALSPE LREKMGKAAI AGAEKIKYEG AGTVEFLVDK HGDFYFMEMN TRIQVEHPVT
     EQVTGFDLIK EQIKVAAGEK ISGKNYAPQA HSIECRINAE DPANDFRPSP GKITTLHIPG
     GPGVRVDTHV YTGYTIPPNY DSMIAKLIVT AETRGEAIKR MKRALNEFVI EGIKTTIPFH
     LRLMDNEVFQ SGHFTTKFME EHTYETL
//
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