ID A0A0F4IWA4_9ACTN Unreviewed; 562 AA.
AC A0A0F4IWA4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KJY25743.1};
GN ORFNames=VR44_31735 {ECO:0000313|EMBL:KJY25743.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY25743.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY25743.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY25743.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KJY25743.1}.
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DR EMBL; JZWV01001030; KJY25743.1; -; Genomic_DNA.
DR RefSeq; WP_045951080.1; NZ_JZWV01001030.1.
DR AlphaFoldDB; A0A0F4IWA4; -.
DR STRING; 68223.GCA_002028425_02586; -.
DR PATRIC; fig|68223.7.peg.3057; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000033551; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 27..143
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 58701 MW; 27351C3C1E982A19 CRC64;
MTHDHDLVLR PTEAQTAAAL APPPGRTGGD LVVETLRGLG ATTVFGLPGQ HALALFDAVG
RSDLRLVGLR TENSAGFAAD AYGRLTGEAV PLLLSTGPGA LMSLPALAEA AAASAPVLAI
SSQVPSPGLG GGRRGHLHEL REQSASFRDV VKSVHTARTP SQIPSVVAEA WESALTAPHG
PVWVEIPEDV LRAETVIPQV TGMDASPREL APRPELTALA AHWLSRAARP VIIAGGGVIR
ADAAGKLKQL AERLNAPVVT TFGGKGAFPW NHPLSLQSWL EDRHMTDFLE DADVLLVVGS
GLGELSSNYH TFFPTGRVVQ IEADLGKLES NHAALGIHAD ARLALQALLE TVGPREDADA
PARVRAVLSD IAARLAAQDL TLEQQLLTSI RSALPARSPS FWDMTILSYW AWSAFDAKHP
NTMHSAQGAG GLGYAFPAAL GAALAEPGSP VLAVSGDGGA MYSVSELATA KQYGLDVTWL
IVDDGGYGIL REYMTDAYDG RTTGTELTRP DFTALAASFG VPASTTTPAT LREDLAAALT
TPGPSVLVLP ATLRMFAPTH LG
//
