ID A0A1Y2EH73_9PEZI Unreviewed; 562 AA.
AC A0A1Y2EH73;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ORY70919.1};
GN ORFNames=BCR38DRAFT_415453 {ECO:0000313|EMBL:ORY70919.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY70919.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY70919.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY70919.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY70919.1}.
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DR EMBL; MCFJ01000001; ORY70919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2EH73; -.
DR STRING; 1141098.A0A1Y2EH73; -.
DR InParanoid; A0A1Y2EH73; -.
DR OrthoDB; 2089851at2759; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
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 GO; GO:0034077; P:butanediol metabolic process; 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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 60388 MW; 99F335D40577A7E3 CRC64;
MPTETVQIVI DSLTAAGVKY VFGVPGAKID SVFNALVDHP EIKVIVCRHE QNAAFIAAAV
GKLTGRPGVC IATSGPGTSN LVTGLITATD EGAPLVAIVG SVKRAQAAKR THQSLRATEL
LTPVTKKVVE AIVEDQVAEV VLDAFRVAAA YPQGATAICL PIDVMTQGMK SSIPAFPASA
FLPPSYGPST DASLQKATKL IQEAKFPVLY LGMRAADEVV VDAVHRFLRK HPVPVIETFQ
AAGAISKELV PLFFGRVSLF RNQPGDKLLT KADLVITVGY DQAEYDANLW NASNHLHIVH
LDCNPATVGY FYNPKLELIG SLASNLDLLT NCLQNVARPQ ETEVAQSILS EFHAWESQAN
ANAKPTGGPV HPLHFIRLLQ SMIDPTTVIA ADVGSVYIWM CRYFYSFHPK TFLVSNAQQT
LGVALPWAIG ASLSQEPEPC SRKVVSVSGD GGFLFSGQEL VTAVKHGCNI THFVWNDGKY
NMVEFQEVDK YGRSSGIELG GVDFAAYAEA FGAKGMKVKS SEQLEGVMRE AMAHKGACVV
DVEIDYADNH ELMTHVVADS VA
//
