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Database: UniProt
Entry: A0A1H6YSI8_9BURK
LinkDB: A0A1H6YSI8_9BURK
Original site: A0A1H6YSI8_9BURK 
ID   A0A1H6YSI8_9BURK        Unreviewed;       580 AA.
AC   A0A1H6YSI8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SEJ44263.1};
GN   ORFNames=SAMN05518853_10268 {ECO:0000313|EMBL:SEJ44263.1};
OS   Variovorax sp. OK202.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEJ44263.1, ECO:0000313|Proteomes:UP000199192};
RN   [1] {ECO:0000313|EMBL:SEJ44263.1, ECO:0000313|Proteomes:UP000199192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK202 {ECO:0000313|EMBL:SEJ44263.1,
RC   ECO:0000313|Proteomes:UP000199192};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; FNZJ01000002; SEJ44263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6YSI8; -.
DR   Proteomes; UP000199192; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          399..548
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   580 AA;  62369 MW;  0EA8DC2B4132658C CRC64;
     MSTSQPAGHL IVECLIEQGM EMAFGVPGES FLAVLDGFHA YRERARFIVN RQEGGAAFMA
     EAHGKLTGRP GVCFVTRGPG ATNASIGVHN AFQDSTPMVL FVGDVGSDFR DREAFQEVDY
     ASFFGPSTKG FAKRVERIDD ANRIPEYIAR AFATAMNGRP GPVVLVLPED MLRSETAARP
     LKRVEAVEPW SDPGALRTLR ELLLKSQRPL VIAGGGGWTT QAAQALQRFA ENWRLPVTNA
     FRFQDTFDNH HPLYAGDVGI AINPKLAQRV KDADLILAIG PRLGEMTTGG YTLLEAPKAK
     QTLVHIHASA EELNRVYQAD LAINAGMSAA ARSLEVLSAP PTLPWEEWTL QAHADYEANL
     VPQALAGMPA ETPRGPVDMA AVVALLQKHL PADAAITNGA GNFASWVHRY FRYHGLTKGA
     KTQLAPTSGA MGYGVPAGIA ANLATGRVAF TIAGDGDFLM TGQELATASQ HGGKSIVVLL
     NNGMFGTIRM HQEREYPERT SGTALRNPDF CGLARAYGYA AERVTETAQF EAALLRALAA
     DTGTLIEIPL DPEVISTRGT LGTITRSAKL QQQQQQQAKG
//
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