ID W1J6I0_9GAMM Unreviewed; 340 AA.
AC W1J6I0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:CDL85653.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CDL85653.1};
GN ORFNames=XSR1_90001 {ECO:0000313|EMBL:CDL85653.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL85653.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL85653.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL85653.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL85653.1}.
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DR EMBL; CBXF010000154; CDL85653.1; -; Genomic_DNA.
DR AlphaFoldDB; W1J6I0; -.
DR STRING; 1427518.XSR1_90001; -.
DR Proteomes; UP000019202; 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: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:UP000019202};
KW Transferase {ECO:0000313|EMBL:CDL85653.1}.
FT DOMAIN 2..113
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 166..314
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 340 AA; 37526 MW; CE568F176A4B7D58 CRC64;
MSGAVPELRR FVAETGMPVV STLKGLGAAD FEHECYLGML GMHGTKAANL AVQACDLLVA
VGARFDDRVT GKLSNFAPHA KVIHLDVDPA EFNKLRQIHV SLQGDVKTLL PHLQQSLSIQ
AWQQEVQQLK NEHAWCYDYQ GEGIYAPLLL KQISDRAPSN TMMTTDVGQH QMWTAQHMSF
SQPENFITSS GLGTMGFGIP AAIGAQLARP QDMVICISGD GSFMMNVQEL GTIKRKQLPI
KIVLLDNQRL GMVRQWQELF FDKRYSETTL TDNPDFLTLA QAFGIPGQRI TEQSQVSGAL
DALFNSEGAY LLHVSIDELE NVWPLVPPGS SNEVMLEKSL
//
