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
//