TKT_PICST
ID TKT_PICST Reviewed; 677 AA.
AC P34736; A3LQC1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT; Synonyms=TKT1; ORFNames=PICST_67105;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7765773; DOI=10.1007/bf00902736;
RA Metzger M., Hollenberg C.;
RT "Isolation and characterization of the Pichia stipitis transketolase gene
RT and expression in a xylose-utilising Saccharomyces cerevisiae
RT transformant.";
RL Appl. Microbiol. Biotechnol. 42:319-325(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA81260.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z26486; CAA81260.2; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000496; ABN64656.1; -; Genomic_DNA.
DR PIR; S37439; S37439.
DR RefSeq; XP_001382685.1; XM_001382648.1.
DR PDB; 5HGX; X-ray; 1.09 A; A=1-677.
DR PDB; 5HJE; X-ray; 1.40 A; A=1-677.
DR PDB; 5HYV; X-ray; 1.03 A; A=1-677.
DR PDB; 5I4I; X-ray; 1.06 A; A=1-677.
DR PDB; 5I51; X-ray; 1.54 A; A=1-677.
DR PDB; 5I5E; X-ray; 1.62 A; A=1-677.
DR PDB; 5I5G; X-ray; 1.95 A; A=1-677.
DR PDB; 5XPS; X-ray; 1.07 A; A=1-677.
DR PDB; 5XQA; X-ray; 1.14 A; A=1-677.
DR PDB; 5XQK; X-ray; 1.12 A; A=1-677.
DR PDB; 5XRV; X-ray; 1.40 A; A=1-677.
DR PDB; 5XRY; X-ray; 1.30 A; A=1-677.
DR PDB; 5XS6; X-ray; 0.97 A; A=1-677.
DR PDB; 5XSA; X-ray; 0.97 A; A=1-677.
DR PDB; 5XSB; X-ray; 0.92 A; A=1-677.
DR PDB; 5XSM; X-ray; 0.97 A; A=1-677.
DR PDB; 5XT0; X-ray; 1.15 A; A=1-677.
DR PDB; 5XT4; X-ray; 1.06 A; A=1-677.
DR PDB; 5XTL; X-ray; 1.10 A; A=1-677.
DR PDB; 5XTV; X-ray; 0.93 A; A=1-677.
DR PDB; 5XTX; X-ray; 1.05 A; A=1-677.
DR PDB; 5XU2; X-ray; 0.97 A; A=1-677.
DR PDB; 5XU9; X-ray; 1.17 A; A=1-677.
DR PDB; 5XUF; X-ray; 0.88 A; A=1-677.
DR PDB; 5XVT; X-ray; 0.85 A; A=1-677.
DR PDBsum; 5HGX; -.
DR PDBsum; 5HJE; -.
DR PDBsum; 5HYV; -.
DR PDBsum; 5I4I; -.
DR PDBsum; 5I51; -.
DR PDBsum; 5I5E; -.
DR PDBsum; 5I5G; -.
DR PDBsum; 5XPS; -.
DR PDBsum; 5XQA; -.
DR PDBsum; 5XQK; -.
DR PDBsum; 5XRV; -.
DR PDBsum; 5XRY; -.
DR PDBsum; 5XS6; -.
DR PDBsum; 5XSA; -.
DR PDBsum; 5XSB; -.
DR PDBsum; 5XSM; -.
DR PDBsum; 5XT0; -.
DR PDBsum; 5XT4; -.
DR PDBsum; 5XTL; -.
DR PDBsum; 5XTV; -.
DR PDBsum; 5XTX; -.
DR PDBsum; 5XU2; -.
DR PDBsum; 5XU9; -.
DR PDBsum; 5XUF; -.
DR PDBsum; 5XVT; -.
DR AlphaFoldDB; P34736; -.
DR SMR; P34736; -.
DR STRING; 4924.XP_001382685.1; -.
DR EnsemblFungi; ABN64656; ABN64656; PICST_67105.
DR GeneID; 4837370; -.
DR KEGG; pic:PICST_67105; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; P34736; -.
DR OMA; HHTEGIE; -.
DR OrthoDB; 354970at2759; -.
DR BRENDA; 2.2.1.1; 4832.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..677
FT /note="Transketolase"
FT /id="PRO_0000191902"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 27
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 566..569
FT /note="AVDA -> SSMT (in Ref. 1; CAA81260)"
FT /evidence="ECO:0000305"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5XUF"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5I5G"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 289..319
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:5XVT"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 501..513
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 562..575
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 588..592
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 596..602
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:5XVT"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 639..645
FT /evidence="ECO:0007829|PDB:5XVT"
FT HELIX 650..664
FT /evidence="ECO:0007829|PDB:5XVT"
SQ SEQUENCE 677 AA; 72805 MW; 7EC1CEA7B23E254A CRC64;
MSSVDQKAIS TIRLLAVDAV AAANSGHPGA PLGLAPAAHA VFKKMRFNPK DTKWINRDRF
VLSNGHACAL LYSMLVLYGY DLTVEDLKKF RQLGSKTPGH PENTDVPGAE VTTGPLGQGI
CNGVGIALAQ AQFAATYNKP DFPISDSYTY VFLGDGCLME GVSSEASSLA GHLQLGNLIA
FWDDNKISID GSTEVAFTED VIARYKSYGW HIVEVSDADT DITAIAAAID EAKKVTNKPT
LVRLTTTIGF GSLAQGTHGV HGAPLKADDI KQLKTKWGFN PEESFAVPAE VTASYNEHVA
ENQKIQQQWN ELFAAYKQKY PELGAELQRR LDGKLPENWD KALPVYTPAD AAVATRKLSE
IVLSKIIPEV PEIIGGSADL TPSNLTKAKG TVDFQPAATG LGDYSGRYIR YGVREHAMGA
IMNGIAAFGA NYKNYGGTFL NFVSYAAGAV RLSALSEFPI TWVATHDSIG LGEDGPTHQP
IETLAHFRAT PNISVWRPAD GNETSAAYKS AIESTHTPHI LALTRQNLPQ LEGSSIEKAS
KGGYTLVQQD KADIIIVATG SEVSLAVDAL KVLEGQGIKA GVVSLPDQLT FDKQSEEYKL
SVLPDGVPIL SVEVMSTFGW SKYSHQQFGL NRFGASGKAP EIFKLFEFTP EGVAERAAKT
VAFYKGKDVV SPLRSAF
