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
//