ID A0A378ARE7_KLEPO Unreviewed; 370 AA.
AC A0A378ARE7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetolactate synthase 2 catalytic subunit {ECO:0000313|EMBL:STV18633.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:STV18633.1};
GN Name=ilvG_1 {ECO:0000313|EMBL:STV18633.1};
GN ORFNames=NCTC5050_02942 {ECO:0000313|EMBL:STV18633.1};
OS Klebsiella pneumoniae subsp. ozaenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=574 {ECO:0000313|EMBL:STV18633.1, ECO:0000313|Proteomes:UP000255382};
RN [1] {ECO:0000313|EMBL:STV18633.1, ECO:0000313|Proteomes:UP000255382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5050 {ECO:0000313|EMBL:STV18633.1,
RC ECO:0000313|Proteomes:UP000255382};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; UGLZ01000005; STV18633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378ARE7; -.
DR Proteomes; UP000255382; Unassembled WGS sequence.
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 GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02015; TPP_AHAS; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000255382};
KW Transferase {ECO:0000313|EMBL:STV18633.1}.
FT DOMAIN 8..143
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 196..344
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 370 AA; 40504 MW; 6AD737328E21C6EF CRC64;
MAFPQAEVAQ ALQMLAQSQQ PMLYVGGGVG MAQAVPALRE FLAVTRMPAT CTLKGLGVVD
ADYPYYLGML GMHGTKAANL AVQECDLLIA VGARFDDRVT GKLNTFAPHA KVIHMDIDPA
ELNKLRQAHI GLTGDLNCLL PALQQPLAID GWRERSAALR AEHAWRYDHP GEAIYAPLLL
KQLSDRKPAD SVVTTDVGQH QMWSAQHMTY TRPENFITSS GLGTMGFGLP AAVGAQVARP
NDTVICISGD GSFMMNVQEL GTVKRKQLPL KIVLLDNQRL GMVRQWQQLF FQERYSETTL
TDNPDFLTLA SAFGIPGQHI TRKDQVEAAL DTMLSSQGPY LLHVSIDELE NVWPLVPPGA
SNSEMLEKLS
//
