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Database: UniProt
Entry: F8PWX3_SERL3
LinkDB: F8PWX3_SERL3
Original site: F8PWX3_SERL3 
ID   F8PWX3_SERL3            Unreviewed;       638 AA.
AC   F8PWX3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=SERLA73DRAFT_182228 {ECO:0000313|EMBL:EGN99300.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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; GL945480; EGN99300.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8PWX3; -.
DR   STRING; 936435.F8PWX3; -.
DR   eggNOG; KOG0523; Eukaryota.
DR   HOGENOM; CLU_028734_0_0_1; -.
DR   InParanoid; F8PWX3; -.
DR   OMA; DMADNTC; -.
DR   OrthoDB; 1691772at2759; -.
DR   Proteomes; UP000008063; 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: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:UP000008063}.
FT   DOMAIN          323..491
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   638 AA;  69782 MW;  AEEB2D80F1EE9F5F CRC64;
     MPGTDSEFPI DLKKYKKLTL DPTKPQLTEE QKSTLLHNIQ LLRDAIVLFT ATGAARGVSG
     HTGGAYDTVP EVCILLSLFE GSDKYLPIMF DEAGHRVATQ YLLSALEGSL PAEHLLHYRE
     ANSKLPGHPE LGLTPGVKFS SGRLGHMWPL VNGIALAHRD KTLFCLGSDG SQQEGNDAEA
     ARLAVAQNLN VKLLIDDNDV TIAGHPSQYL KGYDLTKTLE GHGLKVYTVQ GEDIDALWGA
     ISSIVTYDGP AAVISKRVMA PGIADIEGST HGHDVIPVKA AIKYLTSRGY PESIASDILL
     NIKPASVPYL YIGSTKDVGA NRVIFGEAVN LVLDKLSKEE AAKKVMVIDS DLEGSTGLKV
     IHQKHPEVFV PSGIMERGNF SAAAGFGFDA DKFGVFSTFS AFLEMIISEV TMARLNNCNV
     LCHFSHSGVD EMADNTCHFG VNSLFADNGL SDVQSWLYFP ADPLQMFAVI QRVFFERGIR
     FVFSTRSKVP YILKEDGKTR FFDGDYKFVP GKDETIVEGK AGYVVSFGEM LYRSYDAVLR
     CRQEGLDVGL INKPTLNMVD EPMIKKIGAS PFVLVVESLN QKTGLGSKYG TWLLERQLTP
     KYAYMGTTKE GCGGLSEQIP HQNLDPQAII MRIKQLSQ
//
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