ID J3NSY4_GAET3 Unreviewed; 562 AA. AC J3NSY4; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 24-JAN-2024, entry version 48. DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422}; DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202}; GN Name=20344841 {ECO:0000313|EnsemblFungi:EJT79297}; GN ORFNames=GGTG_04383 {ECO:0000313|EMBL:EJT79297.1}; OS Gaeumannomyces tritici (strain R3-111a-1) (Wheat and barley take-all root OS rot fungus) (Gaeumannomyces graminis var. tritici). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Gaeumannomyces. OX NCBI_TaxID=644352 {ECO:0000313|EMBL:EJT79297.1}; RN [1] {ECO:0000313|Proteomes:UP000006039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R3-111a-1 {ECO:0000313|Proteomes:UP000006039}; RG The Broad Institute Genome Sequencing Platform; RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., RA Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Gaeumannomyces graminis var. tritici strain R3- RT 111a-1."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EJT79297.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R3-111a-1 {ECO:0000313|EMBL:EJT79297.1}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Genome Sequencing Center for Infectious Disease; RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., RA Haas B., Nusbaum C., Birren B.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EJT79297.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R3-111a-1 {ECO:0000313|EMBL:EJT79297.1}; RG The Broad Institute Genome Sequencing Platform; RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.; RT "Annotation of Gaeumannomyces graminis var. tritici R3-111a-1."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EnsemblFungi:EJT79297} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R3-111a-1 {ECO:0000313|EnsemblFungi:EJT79297}; RX PubMed=26416668; DOI=10.1534/g3.115.020057; RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y., RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L., RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B., RA Ma L.-J., Dean R.A.; RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae RT family of fungi."; RL G3 (Bethesda) 5:2539-2545(2015). RN [5] {ECO:0000313|EnsemblFungi:EJT79297} RP IDENTIFICATION. RC STRAIN=R3-111a-1 {ECO:0000313|EnsemblFungi:EJT79297}; RG EnsemblFungi; RL Submitted (APR-2018) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2; CC Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00001041}; CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL385396; EJT79297.1; -; Genomic_DNA. DR RefSeq; XP_009220442.1; XM_009222178.1. DR AlphaFoldDB; J3NSY4; -. DR STRING; 644352.J3NSY4; -. DR EnsemblFungi; EJT79297; EJT79297; GGTG_04383. DR GeneID; 20344841; -. DR VEuPathDB; FungiDB:GGTG_04383; -. DR eggNOG; KOG4166; Eukaryota. DR HOGENOM; CLU_013748_3_2_1; -. DR OrthoDB; 2089851at2759; -. DR Proteomes; UP000006039; 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:UP000006039}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}. FT DOMAIN 6..110 FT /note="Thiamine pyrophosphate enzyme N-terminal TPP- FT binding" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 191..325 FT /note="Thiamine pyrophosphate enzyme central" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 393..542 FT /note="Thiamine pyrophosphate enzyme TPP-binding" FT /evidence="ECO:0000259|Pfam:PF02775" SQ SEQUENCE 562 AA; 60342 MW; AE9D2B3B0265A3EF CRC64; MASQQNTVQV VIDSLKAAGV TIVFGDSVFN ALVDHPEIKV VVCRHEQNAA FIAGAVGKLT DRPGVVIVTS GPGTSNLVTG LVTATDEGSP VVAIAGSVRR VQSARRTHQS LQGVELLRPV TKKVVAALVE DQVAELVADA FRVAATFPRG ATAVSLPIDI MSSTSLTAFP ALPASTFRPP QLGPAPNALL ARTVEMLGRA KFPVLFLGMR ASSARVVEAV HALLRQHPIP VIETFQAAGA ISRELAHLFY GRVGLFRNQA GDRLLARADL VLAIGYDEAE YDSSQWNPTP GRFDIIHMDY QPANVGPNYE PAVELVGSLV ENLRSLTARL ADAGVAVARP QDTDDGRHIF EDFHAWESSE KAVGRPAEGP VHPLQFIRTL QDLIAPESVV TCDVGSVYIY MCRYFYSYTP KTFLVSNAQQ TLGVALPWAI GASLSQDPPC SKKVVSISGD GGFQFSGQEL ATAVLQGCKI AHFIWNDSKY NMVEFQEVDK YGRSAGVELG GVDFVKYAEA YGALGLRART PAELEGVVRE ALAHDGVCLV DVEIDYSSNH ELMQHVIADS VV //