ID A0A0D2ACB7_EXOME Unreviewed; 454 AA.
AC A0A0D2ACB7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN ORFNames=PV10_00420 {ECO:0000313|EMBL:KIV96573.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV96573.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV96573.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV96573.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; KN847520; KIV96573.1; -; Genomic_DNA.
DR EMBL; KN847520; KIV96574.1; -; Genomic_DNA.
DR RefSeq; XP_016228147.1; XM_016364498.1.
DR RefSeq; XP_016228148.1; XM_016364499.1.
DR GeneID; 27318265; -.
DR VEuPathDB; FungiDB:PV10_00420; -.
DR HOGENOM; CLU_013748_0_1_1; -.
DR OMA; GPEQRYN; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000054302; 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; cd02005; TPP_PDC_IPDC; 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; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 92..226
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 289..406
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 454 AA; 50320 MW; A7B11DDF5FD74096 CRC64;
MLLHHTLGNG NFNTFADMAA HIAVDVAKLT DPRDAAAQID HALRECYLQS RPVYLTLPTD
LVKKKVEGER LKTKIDLSAH KNDPAKEDYV VEVVLKYLTE AKSAVILVDS CAVRHRVLDE
AHELIEKSGL PVFVAPMGKG AVDETIPQFG GVYAGDGSNP GVQERVEMAD LLLTIGSVKS
DFNTAGFTYR TSQLKTIDFH STYTRVRYSE YPGVGMKGVL RKLIDRLPQL NIQPGPVPPQ
NITPAEENLD DPAITHDWFW PQLGKWLQEG DIVLTETGTS NYGIFDTRFP KNVTNISQIL
WGSIGYATGS TQGVALAVKE LGSARRTILF TGDGSFQLTA QEVSTMIRHK LKPILFIINN
NGYTIERFIH GMEATYNDIQ PWKYQALLPA FGAQEGSYKT YTVKTKTDVL NLFQDPVFAS
TPYIQLVELF MPEFDAPKGL KITAAAAARR NEKA
//
