Reviewed, UniProtKB/Swiss-Prot P23254 (TKT1_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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)

Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
Cofactor	Binds 1 calcium ion per subunit. Binds 1 thiamine pyrophosphate per subunit.
Subunit structure	Homodimer.
Miscellaneous	Present with 40300 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the transketolase family.

Ontologies

Keywords
Ligand	Calcium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from mutant phenotype. Source: SGD
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct transketolase activity Ref.2 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P43582	1	EBI-19291,EBI-22766
ESS1	P22696	1	EBI-19291,EBI-6679
PRP40	P33203	1	EBI-19291,EBI-701
RSP5	P39940	1	EBI-19291,EBI-16219
SET2	P46995	1	EBI-19291,EBI-16985
URN1	Q06525	1	EBI-19291,EBI-35138

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 680

679

Transketolase 1

PRO_0000191904

Sites

Active site

103

1

Probable

Metal binding

157

1

Calcium

Metal binding

187

1

Calcium

Metal binding

189

1

Calcium; via carbonyl oxygen

Amino acid modifications

Modified residue

248

1

Phosphothreonine Ref.9

Modified residue

335

1

Phosphoserine Ref.9 Ref.7 Ref.8 Ref.10

Modified residue

402

1

Phosphoserine Ref.10

Modified residue

492

1

Phosphoserine Ref.10

Modified residue

639

1

Phosphoserine Ref.10

Experimental info

Mutagenesis

103

1

H → A, F or N: Loss of activity. Ref.13 Ref.14

Mutagenesis

162

1

E → A or Q: Most catalytic properties similar to wild-type. Ref.5

Mutagenesis

382

1

D → A or R: Severe loss of activity. Ref.5

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

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

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)
	P23254-1 [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: 1737042] [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: 8226984] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"The N-terminal amino acid sequence of yeast transketolase." Nixon P.F., Duggleby R.G. Protein Seq. Data Anal. 4:325-326(1991) [PubMed: 1812485] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-36.
[5]	"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: 9119035] [Abstract] Cited for: MUTAGENESIS OF GLU-162 AND ASP-382.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, MASS SPECTROMETRY.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, MASS SPECTROMETRY.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND SER-335, MASS SPECTROMETRY.
[10]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-402; SER-492 AND SER-639, MASS SPECTROMETRY.
[11]	"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: 1628611] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]	"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: 8176731] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[13]	"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: 9398292] [Abstract] Cited for: MUTAGENESIS OF HIS-103, X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[14]	"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: 8521838] [Abstract] Cited for: MUTAGENESIS OF HIS-103.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

XJBYTK. A49510.

RefSeq

NP_015399.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AY0	X-ray	2.60	A/B	1-680	[»]
1GPU	X-ray	1.86	A/B	2-679	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6765N.

IntAct

P23254. 10 interactions.

2-D gel databases

SWISS-2DPAGE

P23254.

Proteomic databases

PeptideAtlas

P23254.

PRIDE

P23254.

Genome annotation databases

Ensembl

YPR074C. Saccharomyces cerevisiae. [Contig view]

GeneID

856188.

GenomeReviews

Gene locus YPR074C in contig U00094_GR.

KEGG

sce:YPR074C.

NMPDR

fig|4932.3.peg.6535.

Organism-specific databases

CYGD

YPR074c.

SGD

S000006278. TKL1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P23254.

OMA

P23254. LVAWESA.

Enzyme and pathway databases

BRENDA

2.2.1.1. 250.

Gene expression databases

ArrayExpress

P23254.

GermOnline

YPR074C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005478. BacTransketolase.
IPR005476. Transketo_C.
IPR005474. Transketo_N.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]

Gene3D

G3DSA:3.40.50.920. Transketo_C_like. 1 hit.

PANTHER

PTHR11624:SF1. BacTransketolase. 1 hit.

Pfam

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

TIGRFAMs

TIGR00232. tktlase_bact. 1 hit.

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

981372.

Entry information

Entry name

TKT1_YEAST

Accession

Primary (citable) accession number: P23254

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)