ID M7TRQ3_EUTLA Unreviewed; 585 AA.
AC M7TRQ3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=UCREL1_324 {ECO:0000313|EMBL:EMR72621.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR72621.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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}.
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DR EMBL; KB705412; EMR72621.1; -; Genomic_DNA.
DR RefSeq; XP_007788290.1; XM_007790099.1.
DR AlphaFoldDB; M7TRQ3; -.
DR STRING; 1287681.M7TRQ3; -.
DR KEGG; ela:UCREL1_324; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OMA; DMCFPGD; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000012174; 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; cd02002; TPP_BFDC; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000012174};
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 210..313
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 415..579
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 585 AA; 62605 MW; 5F79B0F6D77A562A CRC64;
MYTASFAFFE AIWEAGITHC FVNLGSDHPS IIEAMVKGQR EKKDQFPRII TCPNEMVAMS
MADGYARLTG KPQCVIVHVD VGTQGLGAAV HNAGTGRAPV LVFAGLSPFT LEGEMRGSRT
EYIHWIQDVP DQKQIVGQYC RYAAEIKTGK NVKQMVNRAL QFATSDPRGP VYLVGAREVM
EEDIQPYSLD QSVWDPVELG GLTPKAAKAI GEALAGAENP LLITGYSGRN QQVPAALIEL
ADTIKGLRVL DTGGSDMCFP ASHPAWLGLR FGIEPDAIEK SDVIIVLDCD VPWIPAHNKP
RADAQIFHID VDPLKQLMPL FYVPARHRYR ADALVAVEQI TAEAGVAAAK VDAAVFEKQR
VALVASHKAR LDGIAAKAQP AADGTFGTGH LCRTLRTLCP QDTIWAVEAV TNTGFVHDNL
QPELPGSWIN CGGGGLGWSG GGALGIKLAT DAENGGKGKG KFVVQVVGDG TFLFSVPGSV
YWISRRYNIP VLTIVLNNKG WNAPRKSMLL VHPDGLGSTA TNEEINISFD PVPDYAGIAK
AACGGDLFAA KVDKTDHLES TLKEAIAAVQ GGQSAVVDCK VTLNC
//