P23254 (TKT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transketolase 1
Short name=TK 1
EC=2.2.1.1

Gene names

Name:	TKL1
Ordered Locus Names:	YPR074C
ORF Names:	YP9499.29C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Ref.6
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Ref.6 Ref.15 Ref.18
Cofactor	Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+. Ref.13 Binds 1 thiamine pyrophosphate per subunit. Ref.13
Subunit structure	Homodimer.
Miscellaneous	Present with 40300 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the transketolase family.

Ontologies

Keywords
Ligand	Calcium Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pentose-phosphate shunt Inferred from mutant phenotype PubMed 8299150. Source: SGD
Cellular_component	cytoplasm Inferred from sequence or structural similarity PubMed 2843500. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transketolase activity Inferred from mutant phenotype Ref.2. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSP5	P39940	2	EBI-19291,EBI-16219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 680

679

Transketolase 1

PRO_0000191904

Regions

Nucleotide binding

116 – 118

3

Thiamine pyrophosphate

Sites

Active site

418

1

Proton donor Probable

Metal binding

157

1

Magnesium

Metal binding

187

1

Magnesium

Metal binding

189

1

Magnesium; via carbonyl oxygen

Binding site

30

1

Substrate

Binding site

69

1

Thiamine pyrophosphate

Binding site

158

1

Thiamine pyrophosphate; via amide nitrogen

Binding site

187

1

Thiamine pyrophosphate

Binding site

263

1

Substrate

Binding site

263

1

Thiamine pyrophosphate

Binding site

359

1

Substrate

Binding site

386

1

Substrate

Binding site

418

1

Thiamine pyrophosphate

Binding site

445

1

Thiamine pyrophosphate

Binding site

469

1

Substrate

Binding site

477

1

Substrate

Binding site

528

1

Substrate

Site

30

1

Important for catalytic activity

Site

263

1

Important for catalytic activity

Amino acid modifications

Modified residue

248

1

Phosphothreonine Ref.11

Modified residue

335

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

402

1

Phosphoserine Ref.12

Modified residue

492

1

Phosphoserine Ref.12

Modified residue

639

1

Phosphoserine Ref.12

Experimental info

Mutagenesis

30

1

H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. Ref.17

Mutagenesis

30

1

H → N: Loss of activity. Ref.17

Mutagenesis

69

1

H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. Ref.17

Mutagenesis

103

1

H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. Ref.6 Ref.17

Mutagenesis

103

1

H → F: Loss of activity. Ref.6 Ref.17

Mutagenesis

162

1

E → A or Q: Most catalytic properties similar to wild-type. Ref.7

Mutagenesis

263

1

H → A: Strongly reduced catalytic activity. Ref.17

Mutagenesis

359

1

R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. Ref.18

Mutagenesis

382

1

D → A or R: Severe loss of activity. Ref.7

Mutagenesis

469

1

H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. Ref.18

Mutagenesis

477

1

D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. Ref.18

Mutagenesis

481

1

H → A or Q: Reduces catalytic activity by about 95%. Ref.17

Mutagenesis

528

1

R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. Ref.18

Sequence conflict

37 – 38

2

MA → RS in AAA35168. Ref.1

Sequence conflict

45 – 77

33

WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168. Ref.1

Sequence conflict

136 – 143

8

AATYNKPG → DMPLTTSRA in AAA35168. Ref.1

Sequence conflict

232 – 234

3

AQA → RQR in AAA35168. Ref.1

Sequence conflict

243 – 257

15

LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence Ref.1

Sequence conflict

383

1

L → LVLPIL AA sequence Ref.1

Sequence conflict

396

1

D → S in AAA35168. Ref.1

Sequence conflict

528 – 538

11

RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168. Ref.1

Sequence conflict

639 – 680

42

SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168. Ref.1

Secondary structure

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680

Helix Strand Turn

Details...

Helix

6 – 26

21

Helix

32 – 46

15

Beta strand

62 – 67

6

Helix

68 – 70

3

Helix

71 – 80

10

Helix

87 – 90

4

Turn

91 – 94

4

Helix

120 – 139

20

Beta strand

151 – 155

5

Helix

157 – 161

5

Helix

163 – 174

12

Beta strand

180 – 186

7

Beta strand

188 – 190

3

Beta strand

191 – 194

4

Helix

195 – 197

3

Helix

203 – 210

8

Beta strand

213 – 218

6

Turn

220 – 222

3

Helix

224 – 236

13

Beta strand

242 – 247

6

Turn

250 – 253

4

Turn

255 – 258

4

Helix

260 – 262

3

Beta strand

263 – 265

3

Helix

269 – 278

10

Helix

291 – 300

10

Helix

302 – 322

21

Helix

324 – 334

11

Helix

342 – 345

4

Helix

358 – 369

12

Turn

370 – 372

3

Beta strand

376 – 382

7

Helix

384 – 387

4

Beta strand

402 – 406

5

Beta strand

411 – 413

3

Helix

418 – 431

14

Beta strand

436 – 442

7

Helix

443 – 446

4

Helix

447 – 449

3

Helix

450 – 459

10

Beta strand

464 – 468

5

Helix

472 – 474

3

Turn

479 – 481

3

Helix

486 – 491

6

Beta strand

493 – 495

3

Beta strand

497 – 499

3

Helix

504 – 516

13

Beta strand

522 – 525

4

Beta strand

528 – 531

4

Helix

539 – 542

4

Beta strand

547 – 550

4

Beta strand

556 – 561

6

Helix

565 – 577

13

Turn

578 – 580

3

Beta strand

583 – 587

5

Helix

591 – 596

6

Helix

599 – 605

7

Beta strand

608 – 610

3

Beta strand

612 – 615

4

Helix

623 – 625

3

Beta strand

628 – 631

4

Helix

642 – 648

7

Helix

653 – 667

15

Sequences

	Sequence		Length	Mass (Da)
	P23254 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 40225EAA23A63835	FASTA	680	73,806
	10 20 30 40 50 60 MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM NPTNPDWINR 70 80 90 100 110 120 DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT PGHPEFELPG VEVTTGPLGQ 130 140 150 160 170 180 GISNAVGMAM AQANLAATYN KPGFTLSDNY TYVFLGDGCL QEGISSEASS LAGHLKLGNL 190 200 210 220 230 240 IAIYDDNKIT IDGATSISFD EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK 250 260 270 280 290 300 PTLIKMTTTI GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT 310 320 330 340 350 360 ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT AKDSAVATRK 370 380 390 400 410 420 LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP SSGSGNYSGR YIRYGIREHA 430 440 450 460 470 480 MGAIMNGISA FGANYKPYGG TFLNFVSYAA GAVRLSALSG HPVIWVATHD SIGVGEDGPT 490 500 510 520 530 540 HQPIETLAHF RSLPNIQVWR PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE 550 560 570 580 590 600 SASKGGYVLQ DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE 610 620 630 640 650 660 YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG FTPEGVAERA 670 680 QKTIAFYKGD KLISPLKKAF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of the yeast transketolase gene." Fletcher T.S., Kwee I.L., Nakada T., Largman C., Martin B.M. Biochemistry 31:1892-1896(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids." Sundstroem M., Lindqvist Y., Schneider G., Hellman U., Ronne H. J. Biol. Chem. 268:24346-24352(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 208353 / W303-1A.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"The N-terminal amino acid sequence of yeast transketolase." Nixon P.F., Duggleby R.G. Protein Seq. Data Anal. 4:325-326(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-36.
[6]	"His103 in yeast transketolase is required for substrate recognition and catalysis." Wikner C., Meshalnika L., Nilsson U., Baeckstroem S., Lindqvist Y., Schneider G. Eur. J. Biochem. 233:750-755(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-103, FUNCTION, CATALYTIC ACTIVITY.
[7]	"Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis." Meshalkina L., Nilsson U., Wikner C., Kostikowa T., Schneider G. Eur. J. Biochem. 244:646-652(1997) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLU-162 AND ASP-382.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND SER-335, MASS SPECTROMETRY.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-402; SER-492 AND SER-639, MASS SPECTROMETRY.
[13]	"Effect of bivalent cations on the interaction of transketolase with its donor substrate." Sevostyanova I.A., Yurshev V.A., Solovjeva O.N., Zabrodskaya S.V., Kochetov G.A. Proteins 71:541-545(2008) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR.
[14]	"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5-A resolution." Lindqvist Y., Schneider G., Ermler U., Sundstroem M. EMBO J. 11:2373-2379(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[15]	"Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate." Konig S., Schellenberger A., Neef H., Schneider G. J. Biol. Chem. 269:10879-10882(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 3-679 IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE ANALOGS, CATALYTIC ACTIVITY.
[16]	"Refined structure of transketolase from Saccharomyces cerevisiae at 2.0-A resolution." Nikkola M., Lindqvist Y., Schneider G. J. Mol. Biol. 238:387-404(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
[17]	"Identification of catalytically important residues in yeast transketolase." Wikner C., Nilsson U., Meshalkina L., Udekwu C., Lindqvist Y., Schneider G. Biochemistry 36:15643-15649(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE, MUTAGENESIS OF HIS-30; HIS-69; HIS-103; HIS-263 AND HIS-481.
[18]	"Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis." Nilsson U., Meshalkina L., Lindqvist Y., Schneider G. J. Biol. Chem. 272:1864-1869(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-679 IN COMPLEX WITH CALCIUM; D-ERYTHROSE 4-PHOSPHATE AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-359; HIS-469; ASP-477 AND ARG-528.
[19]	"Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae." Fiedler E., Thorell S., Sandalova T., Golbik R., Konig S., Schneider G. Proc. Natl. Acad. Sci. U.S.A. 99:591-595(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-679 IN COMPLEX WITH REACTION INTERMEDIATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63302 Genomic DNA. Translation: AAA35168.1.
X73224 Genomic DNA. Translation: CAA51693.1.
Z49219 Genomic DNA. Translation: CAA89191.1.
Z71255 Genomic DNA. Translation: CAA94982.1.
U51033 Genomic DNA. Translation: AAB68125.1.
BK006949 Genomic DNA. Translation: DAA11494.1.

PIR

XJBYTK. A49510.

RefSeq

NP_015399.1. NM_001184171.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AY0	X-ray	2.60	A/B	1-680	[»]
1GPU	X-ray	1.86	A/B	1-680	[»]
1NGS	X-ray	2.40	A/B	2-679	[»]
1TKA	X-ray	2.70	A/B	3-679	[»]
1TKB	X-ray	2.30	A/B	3-679	[»]
1TKC	X-ray	2.70	A/B	3-679	[»]
1TRK	X-ray	2.00	A/B	1-680	[»]

ProteinModelPortal

P23254.

SMR

P23254. Positions 3-680.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6765N.

IntAct

P23254. 8 interactions.

MINT

MINT-629387.

STRING

4932.YPR074C.

2D gel databases

SWISS-2DPAGE

P23254.

Proteomic databases

PaxDb

P23254.

PeptideAtlas

P23254.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR074C; YPR074C; YPR074C.

GeneID

856188.

KEGG

sce:YPR074C.

Organism-specific databases

SGD

S000006278. TKL1.

Phylogenomic databases

eggNOG

COG0021.

GeneTree

ENSGT00390000005240.

HOGENOM

HOG000225953.

KO

K00615.

OMA

MAVWRPC.

OrthoDB

EOG4V46GV.

Enzyme and pathway databases

SABIO-RK

P23254.

Gene expression databases

Genevestigator

P23254.

GermOnline

YPR074C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.50.920. 1 hit.

InterPro

IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]

SMART

SM00861. Transket_pyr. 1 hit.
[Graphical view]

SUPFAM

SSF52922. Transketo_C_like. 1 hit.

TIGRFAMs

TIGR00232. tktlase_bact. 1 hit.

PROSITE

PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23254.

NextBio

981372.

Entry information

Entry name

TKT1_YEAST

Accession

Primary (citable) accession number: P23254
Secondary accession number(s): D6W478

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program