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Database: UniProt
Entry: W6TWT2_9SPHI
LinkDB: W6TWT2_9SPHI
Original site: W6TWT2_9SPHI 
ID   W6TWT2_9SPHI            Unreviewed;       423 AA.
AC   W6TWT2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   10-APR-2019, entry version 20.
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=N824_14140 {ECO:0000313|EMBL:ETZ24287.1};
OS   Pedobacter sp. V48.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ24287.1, ECO:0000313|Proteomes:UP000019145};
RN   [1] {ECO:0000313|EMBL:ETZ24287.1, ECO:0000313|Proteomes:UP000019145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V48 {ECO:0000313|EMBL:ETZ24287.1,
RC   ECO:0000313|Proteomes:UP000019145};
RX   PubMed=24578271;
RA   Bitzer A.S., Garbeva P., Silby M.W.;
RT   "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT   Coastal Sand Dune in the Netherlands.";
RL   Genome Announc. 2:e00094-14(2014).
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:ETZ24287.1}.
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DR   EMBL; AWRU01000003; ETZ24287.1; -; Genomic_DNA.
DR   STRING; 509635.N824_14140; -.
DR   EnsemblBacteria; ETZ24287; ETZ24287; N824_14140.
DR   PATRIC; fig|509635.5.peg.588; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000019145; 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:UP000019145};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|RuleBase:RU365063, ECO:0000313|EMBL:ETZ24287.1};
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    421       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN       97    294       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   423 AA;  46835 MW;  8E2433B0443CDBDC CRC64;
     MGIKTVAVYS TADRESLHVR FADEAVCIGP PPSKDSYLSI PNIISAAELT NADAIHPGYG
     FLSENAKFSS VCRDYGIKFI GATPEQINSM GDKASAKETM KKAGVPTIPG SEGLLESVKD
     GIKIANGMGY PVILKATAGG GGRGMRVVWK DEEFENAWDS ARQESGAAFG NDALYLEKYI
     EDPRHIEIQI IGDQYGKACH LSERDCSIQR RHQKLVEEAP SPFMTPELRE KMGEAAIKGA
     IAVQYEGAGT IEFLVDKHRN FYFMEMNTRI QVEHPVTEEV INYDLIKEQI KVASGVPISG
     KNYLPDMHAI ECRINAEDPF NNFRPCPGKI TNFHSPGGHG VRVDTHVYAG YQIPSNYDSM
     IAKLICVAQT REEAISTMER ALSEFVIEGV KTTIPFHLKL MKDPNFRAGN FTTKFMETFE
     FSE
//
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