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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//