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Database: UniProt
Entry: G0CL47_XANCA
LinkDB: G0CL47_XANCA
Original site: G0CL47_XANCA 
ID   G0CL47_XANCA            Unreviewed;       680 AA.
AC   G0CL47;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:AEL09126.1};
GN   ORFNames=XCR_4270 {ECO:0000313|EMBL:AEL09126.1};
OS   Xanthomonas campestris pv. raphani 756C.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL09126.1, ECO:0000313|Proteomes:UP000001633};
RN   [1] {ECO:0000313|EMBL:AEL09126.1, ECO:0000313|Proteomes:UP000001633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=756C {ECO:0000313|EMBL:AEL09126.1,
RC   ECO:0000313|Proteomes:UP000001633};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP002789; AEL09126.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0CL47; -.
DR   KEGG; xcp:XCR_4270; -.
DR   PATRIC; fig|990315.4.peg.4023; -.
DR   HOGENOM; CLU_000395_3_1_6; -.
DR   Proteomes; UP000001633; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR048429; MCC_alpha_BT.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF21139; MCC_alpha_BT; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          19..465
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          138..335
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          605..676
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   680 AA;  72680 MW;  5454F78127A3012E CRC64;
     MTQHDMPQHA SITGAGQPYF DKVLIANRGE IACRVIATCR RLGIATVAVY SDADRDARHV
     RLADEAIHIG ASPAQQSYLR GDAILAAARA SGAQAIHPGY GFLSENAGFA DACAQAGVVF
     IGPPAQAIRA MGDKSAAKAL MQRAGVPLTP GYHGDEQAPA FLRAQADAIG YPVLIKASAG
     GGGKGMRRVD ASAAFEDALA SCQREAQSAF GNAHVLVEKY VERPRHIEIQ VFADTHGAVV
     HLFERDCSVQ RRHQKVLEEA PAPGMTEQHR AAMGKAAVDA ARAVGYVGAG TVEFIAGPDG
     DFYFMEMNTR LQVEHPVTEL ITGTDLVDWQ LRVAAGLPLP KRQDELRIHG HALEARLYAE
     DADRGFLPST GTLRQLRLPA ASAHVRIDAG VEQGDTISPY YDPMIAKLIV WDHDRPAALA
     RMRDALAHCH AIGVTTNSAF LARLVSTQAF ATADLDTALI EREQAALFPA PQPPAMAWWC
     LAAVLVAEAA PHAAADPADP FSPWQLADGW RIGAHAARTL VLEAAGERRT LAVRQTADGW
     QVDSADQTHT LRYHAHGEHL RVDMDGRQWR AQILRDGAAI TVLIGAQRAH FQHHDALVEA
     EQPAQAEGGL TAPMPGRVVA LVAQLGEPVR RGQALVVLEA MKMEHTLHAP ADGTVQAYLV
     AEGDLVADGV ALVEFVSASA
//
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