ID A0A0D2BPT7_9EURO Unreviewed; 631 AA.
AC A0A0D2BPT7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW39557.1};
GN ORFNames=PV06_08158 {ECO:0000313|EMBL:KIW39557.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39557.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW39557.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39557.1,
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; KN847339; KIW39557.1; -; Genomic_DNA.
DR RefSeq; XP_016259773.1; XM_016409465.1.
DR AlphaFoldDB; A0A0D2BPT7; -.
DR STRING; 215243.A0A0D2BPT7; -.
DR GeneID; 27360232; -.
DR VEuPathDB; FungiDB:PV06_08158; -.
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 20..150
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 223..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 444..607
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 631 AA; 67685 MW; 69A1FBA0AD74F4E4 CRC64;
MGSMAKKRKV DSAQQEYTTS FAFFEAVWEA GITHVFVNLG SDHPSIMEAI VKGQNEKEGN
FPRIITCPNE MVALSMADGM ARLTNKPQCV IVHVDVGTQG LAAAVHNASC GRAPVLIFAG
LSPYTIEGEY RGSRTEYIHW IQDVPDQKQI VSQYCRYTGE IKAGRNVKQI VNRALQFATS
DPQGPVYLCG AREPMEEDIE PYHLDQGVWH AVGATALPQD AVEMIAKELV KAKEPLMIVG
FTGRNPASVE ANVALADKIP GLRVLDTGGS DMCFPTNHPA ALGLRYGSEP SITTADFILV
VDCDVPWIPT QCKPRADARI VHVDVDPLKQ QMPVFYIPAM ARFKADSATA FSQINDYLSS
SSELTAALSD KSHAAAAKKR QAAYDARWGH FKELAKLPSD PANASIDPHI LGGQIRATVP
EDTIFAVEAV TLTGFIADQI APVLPKSWIN CGGGGLGWSG GGALGVKLAS DFQHRDLASG
DRTGATKGKF VCQIVGDGTF MFSVPSSVYW IAQRYDIPIL TVVLNNKGWN APRRSMLLVH
PDGEGSKVDN KALNISFEPT PDYAGIAKAA SGGKAWAGTV ETVQELLDLL PQAVKAVRDE
GRAAILEVKL GSDLGTKRGV VNGSQVGATS G
//
