ID   D9X3T8_STRVT            Unreviewed;       575 AA.
AC   D9X3T8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:EFL33748.1};
GN   ORFNames=SSQG_04266 {ECO:0000313|EMBL:EFL33748.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL33748.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; GG657757; EFL33748.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9X3T8; -.
DR   STRING; 591159.SSQG_04266; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_2_11; -.
DR   Proteomes; UP000004184; 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; cd02010; TPP_ALS; 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:SF129; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          29..144
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          215..349
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          408..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   575 AA;  61745 MW;  98D1A668CE00BF11 CRC64;
     MVGAGGRTYV RPVSTEGASE SRDTAAVEDV AHLLVRCLRA EGVEYVFGIP GEENIRFVDA
     LQGSGIRYVL VRHEQAASFM AEIYGRLTGR AGVCSATLGP GAINLLLGTA DALTNSAPMV
     ALAAQGSLRR IHKESHQVID LVSMFAPVTQ WAARVECPDA VPEMTRKAFR TAQSERPGAV
     FLAVPEDIEA ERPAEPLAPL QIDAVGADAP SPTQIARAAA VLASARQPVV LAGHGAARAR
     ASAALLRFAE QLNIPVATTF HGKGVFPDDH PNALGAVGFM RHDYGNFGFD TADVLLCVGY
     EIQEFDPAKI NPNGDKRIVH VHRFPAEVDA HYPVAVGVEG DPSQALDALA AALPAGLTYD
     SGSSAKIRTL LDEELQYGRD NDAFPLVPQR VVHDVRAALD RRDIVLADTG AGKMWMSRLY
     PTYEPDTCLV SNGLSTMGFA LPGAIAAKLA LPDRRVLAMM GDGSFLMNSQ ELETAVRERI
     PLVALVLVDE EYGLITWKME LELGRHSHTR FTNPDLVAYA ESFGARGYAV ETADQLLPVL
     RRALDDDSVS VIACPVDYSE NLRLTDRLGS LHGPF
//