ID A0A1I4RPB4_9BURK Unreviewed; 580 AA.
AC A0A1I4RPB4;
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:SFM54006.1};
GN ORFNames=SAMN05444747_106129 {ECO:0000313|EMBL:SFM54006.1};
OS Variovorax sp. OV329.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM54006.1, ECO:0000313|Proteomes:UP000199688};
RN [1] {ECO:0000313|EMBL:SFM54006.1, ECO:0000313|Proteomes:UP000199688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV329 {ECO:0000313|EMBL:SFM54006.1,
RC ECO:0000313|Proteomes:UP000199688};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOUG01000006; SFM54006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4RPB4; -.
DR STRING; 1882825.SAMN05444747_106129; -.
DR Proteomes; UP000199688; 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; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000199688};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 403..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 61544 MW; E059586ACCDE8E67 CRC64;
MALLQMNGAQ VLVRLLLAEQ VRDIYGIVGG KLGPLLHAIA QHEQLRFLGL RHEAAGPMMA
AASCAGSGQI AVALGEMGPG GLNLASGLGV AFNNNLPLVA ITTNQHRAAS YPHSGMFMDL
DTVAVTRPIT KWNAVVHDAR RLPELVRRAF REALGGRPGP VHLDIPQDVL SQACQFDEAE
FAVPPARYRA MGQTRPDGAD VRAAAGLMRR AKRPLIVAGG GVIASGAAER VRELAQRWGA
PVLPTQMALG VVPSDSAHFI GHGGLIAGEP VRQAFDGADL VLAVGCRWSS WMWDEQGPLA
RHARQLISIN IDPSALGAPA LHEVAMQADA GAALDDLLAA CGANLGEDTD RDWLPGLKKS
RQAYEEKLQT LGGQGERGQP MHPAALALAI GEALPADALA VFDGGHTTFW SNDLTPVREV
RTRFHEPGMS HLGFGLPYAI ALQAQQPGRP VALITGDGSF GFTLNELDTA RRYRLPVICI
LHNNAAWGII RAGQRNALGF EMGTALDDTD YAAIARGFGC HGERVTALDE VGPAIRRAMA
SGLPAVIDCQ TRFVPHPAMP AFGSMNRYGF EALSGAEAKH
//
