ID A0A0D2C0Q7_9EURO Unreviewed; 608 AA.
AC A0A0D2C0Q7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW43287.1};
GN ORFNames=PV06_04405 {ECO:0000313|EMBL:KIW43287.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW43287.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW43287.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW43287.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KN847335; KIW43287.1; -; Genomic_DNA.
DR RefSeq; XP_016263503.1; XM_016405297.1.
DR AlphaFoldDB; A0A0D2C0Q7; -.
DR STRING; 215243.A0A0D2C0Q7; -.
DR GeneID; 27356479; -.
DR VEuPathDB; FungiDB:PV06_04405; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000053342; 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; 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:UP000053342};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 21..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..296
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 400..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 608 AA; 65943 MW; E80CC8BABD0A9A73 CRC64;
MPATDLEVAN GATTMIAASA FFDTLDPSRP FPTIITCPSE FVALSAALGY AQVTGIPQCV
LVHVDCGTLA LGQSIHNASV ARVPVLCFAG LSPSTQDGEK VGSRTEYIHW LQDVHDQQAI
VRQYCRYSGE IRISENIKQV TLRALQFSTS DPKGPCYLVA GREVLEQHIE IPDLQGLSMG
PISPTGLPES GVELISHALI NAKRPLIITG YSGRNLRVPP LLAKLCDQLP IRVVETVGSD
LCIRHDHDAY VGFTVRTHPE VLKADVIIVL DCDVPWIPTA GKPAKDVTTF HLDVDPLKQQ
MPLFYINAGK RYRVSSELAI TQLIHFLNQQ NLRQEHHAAA FEERAREARA WRQNLRELEA
PPIDGTIRMP FLAARLRHHV PPQTTYVLEA VTNAAGLVDH LGLVEPGSMY GSGAGGLGWG
GGAALGVKLA KPGSFVCAVL GDGTFFFAQM DSVYWISRRY DIPFLMVVLN NGGWEAPKVS
ALLVNNAGLA SQVSKKTLNI SFEPSPDYPG IAAAAGKAWG RTVTDPKNLD TVLSEAVNVV
KGGISALVEV RCVTHCYTLS KLAVVNQISP PFHNADLGEH SQNSIPVAHV PRCACVNRHF
VGREVNRK
//
