ID B0SKI4_LEPBP Unreviewed; 587 AA.
AC B0SKI4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ABZ96741.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ABZ96741.1};
GN Name=ilvI {ECO:0000313|EMBL:ABZ96741.1};
GN OrderedLocusNames=LEPBI_I0605 {ECO:0000313|EMBL:ABZ96741.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96741.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ96741.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000786; ABZ96741.1; -; Genomic_DNA.
DR RefSeq; WP_012387628.1; NC_010602.1.
DR AlphaFoldDB; B0SKI4; -.
DR STRING; 456481.LEPBI_I0605; -.
DR KEGG; lbi:LEPBI_I0605; -.
DR HOGENOM; CLU_013748_3_1_12; -.
DR OrthoDB; 4494979at2; -.
DR BioCyc; LBIF456481:LEPBI_RS02975-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ABZ96741.1}.
FT DOMAIN 8..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 587 AA; 64363 MW; 98BC2CDE989F0FF1 CRC64;
MKKTGAWLLR FALEEIGVRY TFGIPGVHNT EIYDELNNSN SIQPILVTHE GCGAFMADAI
SRTSHSIGTL VIVPAAGVTH AASGIGEAYL DGIPMLVISG GVRSDSKFKY QLHDMDQHSL
LKPITKQTFK IKSHSEIIET IYQAYQIATS GEPGPVFVEI PVNIQLYAEN VPSIQSYHTY
CNKQTIDPSP PQVQSIAEAV ELLLEAKAPG IFLGWGAVDT TKESIELAEL LVAPVATTLQ
GLSSFPGNHP LFCGMSFGEA AVPAATNAFL HCDCLLAIGT RFSEIATASF GTKVPKNLIH
IDINPDVFNQ NYPSKISIEG DSKIILPILL QKLKERLVFR TGDTNSRMVS LTETIKINKQ
QYIDEWLLHD SKNKVNPCQF FLNLRNRLPD DGFVVVDDGN HTFLTAELMP IHKPRHFISP
TDFNCMGYAV PATIATKLAN PDKDVIGIIG DGAFLMTCME IVTASKNKIG VVFVVFNDGE
LAQIAQAQEI PYNRKTCTIL GTTEFEHIAL ATGAAYIRLE TNDKIKESLQ IAFSLAKEGK
PVILDVSIDY SKKTRFTKGI VGTNLQRLPF ATKVRMIGRA IIRKLTG
//
