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Database: UniProt
Entry: C4R5P8_KOMPG
LinkDB: C4R5P8_KOMPG
Original site: C4R5P8_KOMPG 
ID   C4R5P8_KOMPG            Unreviewed;       707 AA.
AC   C4R5P8;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Transketolase, similar to Tkl2p {ECO:0000313|EMBL:CAY70884.1};
GN   OrderedLocusNames=PAS_chr3_0832 {ECO:0000313|EMBL:CAY70884.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70884.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY70884.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392321; CAY70884.1; -; Genomic_DNA.
DR   RefSeq; XP_002493063.1; XM_002493018.1.
DR   AlphaFoldDB; C4R5P8; -.
DR   SMR; C4R5P8; -.
DR   STRING; 644223.C4R5P8; -.
DR   EnsemblFungi; CAY70884; CAY70884; PAS_chr3_0832.
DR   GeneID; 8199663; -.
DR   KEGG; ppa:PAS_chr3_0832; -.
DR   eggNOG; KOG0523; Eukaryota.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   InParanoid; C4R5P8; -.
DR   OMA; FINIHTV; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000000314; Chromosome 3.
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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          365..547
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   707 AA;  78853 MW;  5B53831AB00D2500 CRC64;
     MARIPKAVST QDDIHELVIK TFRCYVLDLV EQYGGGHPGS AMGMVAIGIA LWKYQMKYAP
     NDPDYFNRDR FVLSNGHVCL FQYLFQHLTG LKEMTVKQLQ SYHSSDYHSL TPGHPEIENP
     AVEVTTGPLG QGISNAVGMA IGSKNLAATY NRPGFPVVDN TIYAIVGDAC LQEGPALESI
     SLAGHLALDN LIVIYDNNQV CCDGSVDVNN TEDISAKFRA QNWNVIDIVD GSRDVATIVK
     AIDWAKAETE RPTLINVRTE IGQDSAFGNH HAAHGSALGE EGIRELKTKY GFNPAQKFWF
     PKEVYDFFAE KPAKGDELVK NWKKLVDSYV KEYPREGQEF LSRVRGELPK NWRTYIPQDK
     PTEPTATRTS AREIVRALGK NLPQVIAGSG DLSVSILLNW DGVKYFFNPK LQTFCGLGGD
     YSGRYIEFGI REHSMCAIAN GLAAYNKGTF LPITSTFYMF YLYAAPALRM AALQELKAIH
     IATHDSIGAG EDGPTHQPIA LSSLFRAMPN FYYMRPADAT EVAALFEVAV ELEHSTLLSL
     SRHEVDQYPG KTSAQGAKRG GYVVEDCEGK PDVQLIGTGS ELEFAIKTAR LLRQQKGWKV
     RVLSFPCQRL FDEQSITYRR SVLRRGEVPT VVVEAYVAYG WERYATAGYT MNTFGKSLPV
     EDVYKYFGYT PEKIGERVVQ YVNSIKASPQ ILYEFHDLKG KPKHDKL
//
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