ID G9IMM4_9BRAD Unreviewed; 124 AA.
AC G9IMM4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AET81742.1};
DE Flags: Fragment;
GN Name=ilvI {ECO:0000313|EMBL:AET81742.1};
OS Bradyrhizobium sp. USDA 3051.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=546898 {ECO:0000313|EMBL:AET81742.1};
RN [1] {ECO:0000313|EMBL:AET81742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA 3051 {ECO:0000313|EMBL:AET81742.1};
RA van Berkum P.B., Elia P., Song Q., Eardly B.D.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AET81742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA 3051 {ECO:0000313|EMBL:AET81742.1};
RX PubMed=22074348; DOI=10.1094/MPMI-09-11-0241;
RA van Berkum P., Elia P., Song Q., Eardly B.D.;
RT "Development and application of a multilocus sequence analysis method for
RT the identification of genotypes within genus Bradyrhizobium and for
RT establishing nodule occupancy of soybean (Glycine max L. Merr).";
RL Mol. Plant Microbe Interact. 25:321-330(2012).
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}.
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DR EMBL; JN685955; AET81742.1; -; Genomic_DNA.
DR AlphaFoldDB; G9IMM4; -.
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 Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
FT DOMAIN 16..118
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AET81742.1"
FT NON_TER 124
FT /evidence="ECO:0000313|EMBL:AET81742.1"
SQ SEQUENCE 124 AA; 13913 MW; 7F161AC3B3124501 CRC64;
LFEATRGKDT YITTEVGQHQ MWAAQFYGFE EPHRWMTSGG LGTMGYGLPA AVGVQVAHPD
SLVIDIAGDA SVQMTMQEMS TAVQYELPIK IFILNNQYMG MVRQWQQLLH GNRLSHSYSE
AMPD
//