ID A0A093Y0N5_9PEZI Unreviewed; 661 AA.
AC A0A093Y0N5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=O988_07212 {ECO:0000313|EMBL:KFX92559.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX92559.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX92559.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX92559.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX92559.1}.
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DR EMBL; JPJR01001664; KFX92559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Y0N5; -.
DR STRING; 1391699.A0A093Y0N5; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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; 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:UP000029329}.
FT DOMAIN 66..198
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 484..611
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 661 AA; 71969 MW; 15D56DA350FFE46F CRC64;
MSVRGVILRL GVYMERVTAF QRVGPFHNAS TFNLLSFASS SKLRRSFSDT PLSASRNVRN
NPKGYTTAFA LFEGLWEAGI TTCFVNVGSD HPSIIEAIVK GKRERPTRWP KFITCPSEIT
AISMADGHAR VTGRPQAVIV HVDVGTQALG QGIHNASIGR VPVFIFAGLC PYTESGELPG
SRTEYMHWLQ ESPDQKAIVR QYCRYTGEIR TGLNVKQTIG RALQFANSTP KGPVYVTSAR
EVLAEEIEPY SLPQEQWVAI GPAALPSDAV HDISTALVQA ERPLIITGYS GRDLRNPELL
VDLANLIPGI RVHDTSGSDV CFPFSHVASE GSRFSTHDCT KDADMILLLD CDVPWIPSRN
PPPKDSKIYH IDSDPLNQQI PVSFFAANGR WKVDSYTALK QLVNHIKDDI SITSALKDPK
YITRGESRAA VHKARIGEIA SKPRLGDGER LDIHNIGSLL KTSLAESTTF VIEAVTSAQT
LYDQLQPDRP GSWINCGGTG IGWSNGAVLG VKMALADLER DKSRKPSLVC QVVGDGSFMC
AAPSSALWVA SKYEIPVLTV VLNNGGWKAP RNSTQLVYPQ GLNTTASDDE INTSFRPTPN
YAALAEAASG SNVGWENTLN NSKSWIKGLR VETVGELKEA LQLANSRVAL EGKGMLIEVS
M
//
