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
//