ID   A0A0D2DP12_9EURO        Unreviewed;       640 AA.
AC   A0A0D2DP12;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=PV06_03023 {ECO:0000313|EMBL:KIW44563.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44563.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW44563.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44563.1,
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   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; KN847334; KIW44563.1; -; Genomic_DNA.
DR   RefSeq; XP_016264779.1; XM_016403774.1.
DR   AlphaFoldDB; A0A0D2DP12; -.
DR   STRING; 215243.A0A0D2DP12; -.
DR   GeneID; 27355097; -.
DR   VEuPathDB; FungiDB:PV06_03023; -.
DR   HOGENOM; CLU_028734_0_0_1; -.
DR   OrthoDB; 1691772at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT   DOMAIN          321..492
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   640 AA;  69732 MW;  272254D8C83AA492 CRC64;
     MVNAKLPVDL SRFKRLSFNP RNNQLSPQEK QDLQHNIGIF RDAIVAFTAT GAARGVAGHT
     GGPFDTAPEV CTLLAMINGS PDNFVDALFD EAGHRVATQY LLAALNGDID PDHLLDYREA
     GSKLPGHPEL GLTPGIKFSS GRLGHMWAMA NGIAMKNKDK TVLLLGSDGS QQEGNDAEAA
     RIAVARRLNV KVFVDNNDVT IAAKPSEYLK GYEIGRTLAG HGLHVVRANG EDLDSLYPKV
     CEVLTHNGPA ALIVDRNMAP HIEGLEGSVK AHDVIPVETA RKYLTSRGYS KEQLSFYDDI
     KPRSNPWKYR GSSKDKIANR MVFGEAVNMV LDALSKEEAA RRVMVIDSDL EGSTGLKAIH
     QKHPEVFIPS GVMERGNFSA AAGFGFKSDG SIQGVFSTFS AFLEMIISEI TMARLNECSV
     LSHFSHSGVD EIADNTCHFG LNHFFADNGL MDAETTTLYF PADAEQMKAV VQKVFFQKGL
     RFIFSTRSKV PLIYKEGTED PLYGEGYDFV PGKDEFIRKG SAGYVVTYGD MLYRSLDAVE
     RLREDGLDVG LVNKPTLNTV DEDSIKIYGS SGFVLVVESI AQKTGLGSRM GTHLLERNLT
     PKYLSMGARK EGGGGLYEQV NEQGLGPDDI VAAIRKVAGK
//