ID A0A014QSP9_9HYPO Unreviewed; 586 AA.
AC A0A014QSP9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetolactate synthase catalytic subunit {ECO:0000313|EMBL:EXU95808.1};
GN ORFNames=X797_011110 {ECO:0000313|EMBL:EXU95808.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU95808.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU95808.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU95808.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) 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:EXU95808.1}.
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DR EMBL; JELW01000064; EXU95808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014QSP9; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000030151; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..313
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..579
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 586 AA; 62137 MW; 5C39B23659F1DE91 CRC64;
MYTASFAFFD ALCGAGVTHC FVNLGSDHPS IIEAMLKGQR EKGAGFPRIV TCPSEMVAMS
MADGFARVTG RPQCVIVHVD VGTQALGVAV HNASVGRAPV LVFAGLSPCT LEGELRGSRT
EFIHWLQDIP DQKAIVGQYC RYAAEIKTGA NMKQMVNRAL QFATSGPQGP VYLCATREVL
EADLAPYEIQ QDQWDPVELG GLSPRSADSI AEALARAQRP LVITGYSGRN LQIPPVLVRL
ADAVKALRVL DGSGSDMCFP ANHPAWLGMR IGAHAAVEEA DVILVLDCDV PWIPTRCRPK
RDAAIFHIDV DPLKQQMPLF YIPAQARYRA DALMALEQIL GALTGGHAAK VLAEGDAAAA
EEARNASHAQ FLAQIAHAAR PFANGSFGTG YLSSLLRRVC PEETIWAVEA VTNTTFIHDN
IQPTVPGSWI NCGGGGLGWS GGGALGIKLA TDAQAGGAGK GKFVCQIVGD GTYLFSMPSS
VYWISKRYSI PVLTIVLNND GWNAPRKSYM LVHPDGEAAS ATNENINISF SPAPDYAGLA
AAAGSGDIHA FRVSKANELG SVLEQAVAKV LGGQTAVVDC KVVLDC
//
