ID A0A094E2G1_9PEZI Unreviewed; 588 AA.
AC A0A094E2G1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY41302.1};
GN ORFNames=V494_03071 {ECO:0000313|EMBL:KFY41302.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY41302.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY41302.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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 -!- 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, ECO:0000256|RuleBase:RU362132}.
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:KFY41302.1}.
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DR EMBL; JPJW01001014; KFY41302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094E2G1; -.
DR STRING; 1420907.A0A094E2G1; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000029288; 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; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR045025; HACL1-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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:UP000029288};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..561
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 62137 MW; 41ADB3C27440D324 CRC64;
MAAPTGAQLI ARALHELGIK VIFGLVGIPV VQIAEEAIKL GIRFIAFRNE QAASYAATAY
GYLTGKPGVC LVVGGPGVLH AMSGIGNSSA NAWPLLLLAG SSESHLVTKG AFQELDAISL
LTPHVKLAVR STIDSIPQSI SNAYRTSWYG RGGTGFVDLP ADVIQGEGDE ISKVVIPSPA
RAAGDPERIT AAVKLLKSAK APLVIVGKGA AYAQAEGGIR RLVDETKVPF LPTPMGKGVL
ADSHPSNTAS ARSAALKGAD VVLVLGARLN WILHFGEEPK WNPDVKIIQV DISAEELGKN
NGDASISIIG DINLVTSQIS AGLQNWQYNT STPYISAIQA STTKNEATAA KSAQVDKIPM
TYGRTFAVIK ETLNALSPPE NGEIVYVSEG ANTMDISRSV FNVEHPRLRL DAGTYATMGV
GLGYAIAAHC AYNLPDPQAT SGPSSSRKKI VCLEGDSAFG FSMPEIETMA RYCMDVLVFV
VNNGGVYHGD SADSDAWLAL QDKTTQGAAG GLRSTSLGWE VGYEKMAEMC GGKGYLVRTP
EELRKATEEG FKATVPVVIN IIIEAGQAKK LEFAWQKSTQ KKPKNAKL
//