ID   R7Z3C0_CONA1            Unreviewed;       724 AA.
AC   R7Z3C0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=W97_07760 {ECO:0000313|EMBL:EON68436.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON68436.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) 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; JH767596; EON68436.1; -; Genomic_DNA.
DR   RefSeq; XP_007783753.1; XM_007785563.1.
DR   AlphaFoldDB; R7Z3C0; -.
DR   STRING; 1168221.R7Z3C0; -.
DR   GeneID; 19905071; -.
DR   eggNOG; KOG0523; Eukaryota.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   OMA; GHASMFL; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000016924; 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   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
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; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 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.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          401..575
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   724 AA;  78839 MW;  C3CEBC2AFF87D53B CRC64;
     MAPQLAEFDH TTFTTTSQLK KSAHLTNGFS HHEDIRDENP EQDLSDDEFA TISIRNLVHD
     LCMQNGGGHG GSALGMAAIG VALWKYEMRY NPCDPEWFDR DRFVLSNGHA SMFLYTMNHL
     VGYNVWTMEQ LKGYGAAKLN GYTTISHAHP EIEVPGVEVT TGPLGQGIAN SVGLAIASKN
     LAATFNKPGF DVVRSRIYCT TGDGCLMEGV ALEAIALAGH LQLDNLVLLY DNNQVTCDGP
     LEWVNSEDIN TKMRACGWEV LDVLDGTNDV QTIVSALSYA KRLVGKPVFI NIRTVIGAGT
     AAAGTAKAHH GVFDKESVAK SKALTGLDPE KSHVVPQRAL DFFRERRAAG TALAKTWSDL
     LARYAERFPE LHESLDARRR GICGDFDQVL SGIDSQQLRG LATRESNGVI LEKLWKSCPA
     LCGGGADLAN SNKITYAETD VFHPLTGYKG RYLRHGIREH AMASIANGLA AYSPGTFLPI
     TATFLIFYIY AAPGVRMGAL SGLQVIHIAT HDSFGEGQNG PTHQPVEIDS LYRAMPSLQY
     LRPCDAEELV GCWQIALSAR HQPSMLSLGR DPVGQVPNTS RDKVKLGAYM VAEEADADVT
     LASCGTNLHY VVSAAELLKK RHGIKARLVS APSLDLFQLQ DEHYRAAIFP LDGKPVISVE
     EYVATTWARY VTASIGMTSY GYSASNESNY QRFGLDAKGI EGKVVAYLAK LQGQNARTAG
     WHQL
//