ID E3S0B8_PYRTT Unreviewed; 593 AA.
AC E3S0B8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=PTT_15486 {ECO:0000313|EMBL:EFQ88595.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ88595.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ88595.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL536294; EFQ88595.1; -; Genomic_DNA.
DR RefSeq; XP_003303323.1; XM_003303275.1.
DR AlphaFoldDB; E3S0B8; -.
DR STRING; 861557.E3S0B8; -.
DR EnsemblFungi; EFQ88595; EFQ88595; PTT_15486.
DR KEGG; pte:PTT_15486; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000001067; 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:UP000001067};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..314
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 414..567
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 593 AA; 64636 MW; F302530FC4A65C6B CRC64;
MVYTASFAFF EALWEYGVSH VFVNLGSDHP SIIEAIVKGQ NEKKGQFPKI ITCPNEMVAL
SMADGYARLT GKPQCVIVHV DVGTQGLGAA VHNASCGRAP VLIFAGLSPF TIEGEMRGSR
TEYIHWIQDV PDQKQIVAQY CRYTGEIKSG RNVKQMVNRA LSFAMSDPKG PVYLYGAREP
MEEDLTPYKL DMDYWQPVEP AALPPSGVKT IAEALAHAQE PLIVTGYSGR NHDAVQELVR
LADNIKGIRV LDTGGSDMCF PANHPAWLGL RYGNDPAIKS ADVILVLDCD VPWINTQCHP
KDSAKIFHVD VDPLKQQMPV FYLNATQRYR ADSYTSLTQL NEYLESALKE KLSSQLFSQR
WSALQESHKK KLDGIANEAK VDDNGHFSTP YLCSQLNKFC PNDTIWAIEA VTQTGFVADQ
IQATLPGSWI NCGGGGLGWS GGGALGIKLA TETEGKKQFV CQIVGDGTYL FSVPGSVYWI
SQRYQIPILT IVLNNKGWNA PRRSMLLVHP DGEGSKVSNE ELNISFAPTP DYSGIAKAAS
GGEIWAAHAS TAEELGKLLP EAIKSVLEGK SAVLDAHLEG PEGKYGGAKG RLG
//