TKT1_YEAST
ID TKT1_YEAST Reviewed; 680 AA.
AC P23254; D6W478;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1;
GN Name=TKL1; OrderedLocusNames=YPR074C; ORFNames=YP9499.29C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1737042; DOI=10.1021/bi00121a044;
RA Fletcher T.S., Kwee I.L., Nakada T., Largman C., Martin B.M.;
RT "DNA sequence of the yeast transketolase gene.";
RL Biochemistry 31:1892-1896(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=8226984; DOI=10.1016/s0021-9258(20)80532-8;
RA Sundstroem M., Lindqvist Y., Schneider G., Hellman U., Ronne H.;
RT "Yeast TKL1 gene encodes a transketolase that is required for efficient
RT glycolysis and biosynthesis of aromatic amino acids.";
RL J. Biol. Chem. 268:24346-24352(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 2-36.
RX PubMed=1812485;
RA Nixon P.F., Duggleby R.G.;
RT "The N-terminal amino acid sequence of yeast transketolase.";
RL Protein Seq. Data Anal. 4:325-326(1991).
RN [6]
RP MUTAGENESIS OF HIS-103, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8521838; DOI=10.1111/j.1432-1033.1995.750_3.x;
RA Wikner C., Meshalnika L., Nilsson U., Baeckstroem S., Lindqvist Y.,
RA Schneider G.;
RT "His103 in yeast transketolase is required for substrate recognition and
RT catalysis.";
RL Eur. J. Biochem. 233:750-755(1995).
RN [7]
RP MUTAGENESIS OF GLU-162 AND ASP-382.
RX PubMed=9119035; DOI=10.1111/j.1432-1033.1997.t01-1-00646.x;
RA Meshalkina L., Nilsson U., Wikner C., Kostikowa T., Schneider G.;
RT "Examination of the thiamin diphosphate binding site in yeast transketolase
RT by site-directed mutagenesis.";
RL Eur. J. Biochem. 244:646-652(1997).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-402 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP COFACTOR.
RX PubMed=18186462; DOI=10.1002/prot.21880;
RA Sevostyanova I.A., Yurshev V.A., Solovjeva O.N., Zabrodskaya S.V.,
RA Kochetov G.A.;
RT "Effect of bivalent cations on the interaction of transketolase with its
RT donor substrate.";
RL Proteins 71:541-545(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1628611; DOI=10.1002/j.1460-2075.1992.tb05301.x;
RA Lindqvist Y., Schneider G., Ermler U., Sundstroem M.;
RT "Three-dimensional structure of transketolase, a thiamine diphosphate
RT dependent enzyme, at 2.5-A resolution.";
RL EMBO J. 11:2373-2379(1992).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 3-679 IN COMPLEX WITH CALCIUM AND
RP THIAMINE PYROPHOSPHATE ANALOGS, AND CATALYTIC ACTIVITY.
RX PubMed=8144674; DOI=10.1016/s0021-9258(17)34140-6;
RA Konig S., Schellenberger A., Neef H., Schneider G.;
RT "Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes.
RT Crystal structures of yeast transketolase in complex with analogs of
RT thiamin diphosphate.";
RL J. Biol. Chem. 269:10879-10882(1994).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE
RP PYROPHOSPHATE.
RX PubMed=8176731; DOI=10.1006/jmbi.1994.1299;
RA Nikkola M., Lindqvist Y., Schneider G.;
RT "Refined structure of transketolase from Saccharomyces cerevisiae at 2.0-A
RT resolution.";
RL J. Mol. Biol. 238:387-404(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE
RP PYROPHOSPHATE, AND MUTAGENESIS OF HIS-30; HIS-69; HIS-103; HIS-263 AND
RP HIS-481.
RX PubMed=9398292; DOI=10.1021/bi971606b;
RA Wikner C., Nilsson U., Meshalkina L., Udekwu C., Lindqvist Y.,
RA Schneider G.;
RT "Identification of catalytically important residues in yeast
RT transketolase.";
RL Biochemistry 36:15643-15649(1997).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-679 IN COMPLEX WITH CALCIUM;
RP D-ERYTHROSE 4-PHOSPHATE AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ARG-359; HIS-469; ASP-477 AND ARG-528.
RX PubMed=8999873; DOI=10.1074/jbc.272.3.1864;
RA Nilsson U., Meshalkina L., Lindqvist Y., Schneider G.;
RT "Examination of substrate binding in thiamin diphosphate-dependent
RT transketolase by protein crystallography and site-directed mutagenesis.";
RL J. Biol. Chem. 272:1864-1869(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-679 IN COMPLEX WITH REACTION
RP INTERMEDIATE.
RX PubMed=11773632; DOI=10.1073/pnas.022510999;
RA Fiedler E., Thorell S., Sandalova T., Golbik R., Konig S., Schneider G.;
RT "Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal
RT structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin
RT diphosphate in the active site of transketolase from Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:591-595(2002).
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:0000269|PubMed:8521838}.
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 Evidence={ECO:0000269|PubMed:8144674, ECO:0000269|PubMed:8521838,
CC ECO:0000269|PubMed:8999873};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18186462};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:18186462};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18186462};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18186462};
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+).
CC {ECO:0000269|PubMed:18186462};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:18186462};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:18186462};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11773632,
CC ECO:0000269|PubMed:8144674, ECO:0000269|PubMed:8176731,
CC ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292}.
CC -!- INTERACTION:
CC P23254; P39940: RSP5; NbExp=2; IntAct=EBI-19291, EBI-16219;
CC P23254; P33315: TKL2; NbExp=3; IntAct=EBI-19291, EBI-19297;
CC -!- MISCELLANEOUS: Present with 40300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; M63302; AAA35168.1; -; Genomic_DNA.
DR EMBL; X73224; CAA51693.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89191.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94982.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68125.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11494.1; -; Genomic_DNA.
DR PIR; A49510; XJBYTK.
DR RefSeq; NP_015399.1; NM_001184171.1.
DR PDB; 1AY0; X-ray; 2.60 A; A/B=1-680.
DR PDB; 1GPU; X-ray; 1.86 A; A/B=1-680.
DR PDB; 1NGS; X-ray; 2.40 A; A/B=1-680.
DR PDB; 1TKA; X-ray; 2.70 A; A/B=3-680.
DR PDB; 1TKB; X-ray; 2.30 A; A/B=3-680.
DR PDB; 1TKC; X-ray; 2.70 A; A/B=3-680.
DR PDB; 1TRK; X-ray; 2.00 A; A/B=1-680.
DR PDBsum; 1AY0; -.
DR PDBsum; 1GPU; -.
DR PDBsum; 1NGS; -.
DR PDBsum; 1TKA; -.
DR PDBsum; 1TKB; -.
DR PDBsum; 1TKC; -.
DR PDBsum; 1TRK; -.
DR AlphaFoldDB; P23254; -.
DR SMR; P23254; -.
DR BioGRID; 36247; 219.
DR DIP; DIP-6765N; -.
DR IntAct; P23254; 13.
DR MINT; P23254; -.
DR STRING; 4932.YPR074C; -.
DR iPTMnet; P23254; -.
DR SWISS-2DPAGE; P23254; -.
DR MaxQB; P23254; -.
DR PaxDb; P23254; -.
DR PRIDE; P23254; -.
DR TopDownProteomics; P23254; -.
DR EnsemblFungi; YPR074C_mRNA; YPR074C; YPR074C.
DR GeneID; 856188; -.
DR KEGG; sce:YPR074C; -.
DR SGD; S000006278; TKL1.
DR VEuPathDB; FungiDB:YPR074C; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000176704; -.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; P23254; -.
DR OMA; HHTEGIE; -.
DR BioCyc; YEAST:YPR074C-MON; -.
DR BRENDA; 2.2.1.1; 984.
DR SABIO-RK; P23254; -.
DR EvolutionaryTrace; P23254; -.
DR PRO; PR:P23254; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P23254; protein.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IMP:SGD.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:SGD.
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; Direct protein sequencing; Isopeptide bond;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1812485"
FT CHAIN 2..680
FT /note="Transketolase 1"
FT /id="PRO_0000191904"
FT ACT_SITE 418
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 30
FT /ligand="substrate"
FT BINDING 69
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 116..118
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 158
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 187
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 263
FT /ligand="substrate"
FT BINDING 263
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 359
FT /ligand="substrate"
FT BINDING 386
FT /ligand="substrate"
FT BINDING 418
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 445
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:8176731,
FT ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292"
FT BINDING 469
FT /ligand="substrate"
FT BINDING 477
FT /ligand="substrate"
FT BINDING 528
FT /ligand="substrate"
FT SITE 30
FT /note="Important for catalytic activity"
FT SITE 263
FT /note="Important for catalytic activity"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 30
FT /note="H->A,Q: Strongly reduced catalytic activity.
FT Decreases affinity for xylulose 5-phosphate about 15
FT times."
FT /evidence="ECO:0000269|PubMed:9398292"
FT MUTAGEN 30
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9398292"
FT MUTAGEN 69
FT /note="H->A: Reduces catalytic activity by about 98%.
FT Decreased affinity for donor substrate."
FT /evidence="ECO:0000269|PubMed:9398292"
FT MUTAGEN 103
FT /note="H->A,N: Reduces activity by over 96% and decreases
FT affinity for thiamine pyrophosphate and xylulose 5-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:8521838,
FT ECO:0000269|PubMed:9398292"
FT MUTAGEN 103
FT /note="H->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8521838,
FT ECO:0000269|PubMed:9398292"
FT MUTAGEN 162
FT /note="E->A,Q: Most catalytic properties similar to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:9119035"
FT MUTAGEN 263
FT /note="H->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:9398292"
FT MUTAGEN 359
FT /note="R->A: Slightly reduced affinity for xylulose 5-
FT phosphate and strongly reduced affinity for ribose 5-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:8999873"
FT MUTAGEN 382
FT /note="D->A,R: Severe loss of activity."
FT /evidence="ECO:0000269|PubMed:9119035"
FT MUTAGEN 469
FT /note="H->A: Strongly reduced affinity for xylulose 5-
FT phosphate and ribose 5-phosphate."
FT /evidence="ECO:0000269|PubMed:8999873"
FT MUTAGEN 477
FT /note="D->A: Strongly reduced catalytic activity. Strongly
FT reduced affinity for xylulose 5-phosphate and ribose 5-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:8999873"
FT MUTAGEN 481
FT /note="H->A,Q: Reduces catalytic activity by about 95%."
FT /evidence="ECO:0000269|PubMed:9398292"
FT MUTAGEN 528
FT /note="R->A: Reduced affinity for xylulose 5-phosphate and
FT strongly reduced affinity for ribose 5-phosphate."
FT /evidence="ECO:0000269|PubMed:8999873"
FT CONFLICT 37..38
FT /note="MA -> RS (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..77
FT /note="WSQMRMNPTNPDWINRDRFVLSNGHAVALLYSM -> GESNAHEPNQPKTGS
FT TEIDLSCLTVTRSLCCIY (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..143
FT /note="AATYNKPG -> DMPLTTSRA (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..234
FT /note="AQA -> RQR (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..257
FT /note="LIKMTTTIGYGSLHA -> FDQNDHNHWLRFLRS (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> LVLPIL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="D -> S (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..538
FT /note="RQNLPQLEGSS -> PDKTCHNWKVAL (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..680
FT /note="SGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF -> PVRHQK
FT SSSSSVSPQKVLLKELKRPLHSIRVTS (in Ref. 1; AAA35168)"
FT /evidence="ECO:0000305"
FT HELIX 6..26
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1TKB"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 302..322
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:1TRK"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 565..577
FT /evidence="ECO:0007829|PDB:1GPU"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 591..596
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:1GPU"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:1GPU"
FT HELIX 653..667
FT /evidence="ECO:0007829|PDB:1GPU"
SQ SEQUENCE 680 AA; 73806 MW; 40225EAA23A63835 CRC64;
MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM NPTNPDWINR
DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT PGHPEFELPG VEVTTGPLGQ
GISNAVGMAM AQANLAATYN KPGFTLSDNY TYVFLGDGCL QEGISSEASS LAGHLKLGNL
IAIYDDNKIT IDGATSISFD EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK
PTLIKMTTTI GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT
ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT AKDSAVATRK
LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP SSGSGNYSGR YIRYGIREHA
MGAIMNGISA FGANYKPYGG TFLNFVSYAA GAVRLSALSG HPVIWVATHD SIGVGEDGPT
HQPIETLAHF RSLPNIQVWR PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE
SASKGGYVLQ DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE
YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG FTPEGVAERA
QKTIAFYKGD KLISPLKKAF
