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Database: UniProt
Entry: I0XS73_9LEPT
LinkDB: I0XS73_9LEPT
Original site: I0XS73_9LEPT 
ID   I0XS73_9LEPT            Unreviewed;       913 AA.
AC   I0XS73;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Biotin carboxylase C-terminal domain / biotin-requiring enzyme multi-domain protein {ECO:0000313|EMBL:EIE01731.1};
GN   ORFNames=LEP1GSC185_2998 {ECO:0000313|EMBL:EIE01731.1};
OS   Leptospira licerasiae serovar Varillal str. VAR 010.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE01731.1, ECO:0000313|Proteomes:UP000004889};
RN   [1] {ECO:0000313|EMBL:EIE01731.1, ECO:0000313|Proteomes:UP000004889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VAR 010 {ECO:0000313|EMBL:EIE01731.1};
RX   PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA   Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA   Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA   Vinetz J.M., Matthias M.A.;
RT   "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT   Leptospiral Evolution and Pathogenicity.";
RL   PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIE01731.1}.
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DR   EMBL; AHOO02000006; EIE01731.1; -; Genomic_DNA.
DR   RefSeq; WP_008590768.1; NZ_AHOO02000006.1.
DR   AlphaFoldDB; I0XS73; -.
DR   PATRIC; fig|1049972.3.peg.1819; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000004889; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR48095:SF4; BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
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; 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          25..589
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          221..446
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          798..888
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   913 AA;  102105 MW;  3331562C2C3F737B CRC64;
     MIDYQNRRIT FRESTSPWIH SFSLETIKCL IVCRGPVRKE AMEIFDQIGV REYGILLSEK
     DSVVYPMALA PELRDFRFPS NIHRVPDYMG AGAEEKAARI KQIIQIAKDN GYTHIFAGYG
     FMAEDSEFIE AIEESGVTFM GPSSHVAHQA GSKDEAKKLA RKLNVSVTPG VDTISATCLL
     KKAKDEKALV ALAKEKGLNF SYNSSISLEE NAEALLYAGY EKIVELVTIP ELQAQAEIEA
     AEIWKKYPSN RIRFKYVGGG GGKGQRVVSK PEEVKTAVQE ILSESKVTAP GSNRNFLIEL
     NIEKTRHNEI QLIGNGEWCL ALGGRDCSVQ MHEQKLLEIS LTQELLQNEI AILEKTSPKK
     AEIMKADLQV LKEMEEQSER FGQAVALNSV STFELIVEGT NHFFMEMNTR IQVEHRVTEM
     VYSLKFTNPE NKSEFFIVDS LIEAMALLAL HGKRLPKPER VVRNISGAEV RINATNKAIQ
     PHAGGVILSW SKPLPEEIRD DQGISVRNPD TGLFVHYKVA GAYDSNIALL ITYGTSREDN
     LRRLGNILRK TELRGQDLQT NLLVHYGLIH WILGKDPLFK PSTAFMISYL AAVGALESLG
     KDIDLEVAWT KVLSNAPAEG KKVLSRKLTL ITRPLGEILA DAHVLAGFLG YHENVSWKFE
     KDQVVWLRNP IHILSDLYYY LHMEGELHQS PSEQIWDHDQ KILQSALAFY DELERLTGKK
     ADSADWDSVL AAKAPAGVDA GIWTKAIASH KGFQIGLELL KLIPNLGNKS GFYKLGVDEN
     LEPVIPEEFK KADTRDAFIK FLAPAPKASS DEIVSPMGGM FYSKEAPDLP PMVNEGEHFK
     AGQPLFIVEV MKMFNKITAP FSGTVKEVIL KESDGKIIQK GQTIFKIVPD EIIKIETPEE
     IQDRKNKVTF SLL
//
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