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Database: UniProt
Entry: F3Z6A2_9ACTN
LinkDB: F3Z6A2_9ACTN
Original site: F3Z6A2_9ACTN 
ID   F3Z6A2_9ACTN            Unreviewed;       558 AA.
AC   F3Z6A2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Putative acetolactate synthase {ECO:0000313|EMBL:EGJ77226.1};
GN   ORFNames=STTU_4437 {ECO:0000313|EMBL:EGJ77226.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ77226.1};
RN   [1] {ECO:0000313|EMBL:EGJ77226.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ77226.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CM001165; EGJ77226.1; -; Genomic_DNA.
DR   RefSeq; WP_007826748.1; NZ_CM001165.1.
DR   AlphaFoldDB; F3Z6A2; -.
DR   HOGENOM; CLU_013748_3_1_11; -.
DR   Proteomes; UP000003955; Chromosome.
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; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-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..144
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          408..547
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  58490 MW;  E7E7358CB0D5F259 CRC64;
     MSHDHDIELR PTEAQTRAAL DPPAGRTGGD LVVETLHGLG ATTVFGLPGQ HALALFDAVR
     RSSLAYVGLR VENNAAFAAD GYGRVTGEAA PLLLSTGPGA LTSLSALQEA AASSSPVLAI
     CSQVPAAGLG GGRHGYLHEL RDQQGSVRDI VKSVHVVRAA SQIPSAIAAA WESALSAPHG
     PVWVEIPQDV LAAETLLPEV NAPDALPEPL VPRPELTALA ADWLAHAERP VVLAGGGVVR
     ADAAGKLRAL AEHMNLPVVT TYGGKGAFPW EHPLSGQSWM EDRHTTDFLA DADVLLVVGS
     GLGELSSHYH SLAPGGRIIQ IEADLGKLEA NHRALGIHAD ARLALQALLE TAPPREDPEA
     PARVAELLRK VRARLDAQDL SRERELLTTI RAALPDDSPS FWDMTILGYW AWAGFDPRGP
     GTMHTAQGAG GLGLAFPAAL GAAVADPTRP VLAVTGDGGA MYSLAELATA RQHGLPVTWL
     VVDDGGYGIL REYLTGAYGE AVGTELSRPD FVALAESFGV PALTTTATDL GKDLAEALES
     GEPRVVVLRE RLRMFEES
//
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