UniProtKB - P23254 (TKT1_YEAST)

>sp|P23254|TKT1_YEAST Transketolase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=TKL1 PE=1 SV=4
MTQFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNPTNPDWINR
DRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPGHPEFELPGVEVTTGPLGQ
GISNAVGMAMAQANLAATYNKPGFTLSDNYTYVFLGDGCLQEGISSEASSLAGHLKLGNL
IAIYDDNKITIDGATSISFDEDVAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDK
PTLIKMTTTIGYGSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKT
ILKPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQLPANWESKLPTYTAKDSAVATRK
LSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSSGSGNYSGRYIRYGIREHA
MGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLSALSGHPVIWVATHDSIGVGEDGPT
HQPIETLAHFRSLPNIQVWRPADGNEVSAAYKNSLESKHTPSIIALSRQNLPQLEGSSIE
SASKGGYVLQDVANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLE
YRLSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFTPEGVAERA
QKTIAFYKGDKLISPLKKAF

Entry version 208 (10 Feb 2021)
Sequence version 4 (23 Jan 2007)
Previous versions | rss

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Protein

Transketolase 1

Gene

TKL1

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

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.1 Publication

Miscellaneous

Present with 40300 molecules/cell in log phase SD medium.1 Publication

Catalytic activityⁱ

D-glyceraldehyde 3-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
D-sedoheptulose 7-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
aldehydo-D-ribose 5-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
D-xylulose 5-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.16
  "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.
- Ref.19
  "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.
EC:
2.2.1.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.16
  "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.
- Ref.19
  "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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
D-glyceraldehyde 3-phosphate
zoom
+
D-sedoheptulose 7-phosphate
zoom
=
aldehydo-D-ribose 5-phosphate
zoom
+
D-xylulose 5-phosphate
zoom

Cofactorⁱ

Protein has several cofactor binding sites:

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	30	Substrate	1
Siteⁱ	30	Important for catalytic activity	1
Binding siteⁱ	69	Thiamine pyrophosphate3 Publications	1
Metal bindingⁱ	157	Magnesium	1
Binding siteⁱ	158	Thiamine pyrophosphate; via amide nitrogen3 Publications	1
Metal bindingⁱ	187	Magnesium	1
Binding siteⁱ	187	Thiamine pyrophosphate3 Publications	1
Metal bindingⁱ	189	Magnesium; via carbonyl oxygen	1
Binding siteⁱ	263	Substrate	1
Binding siteⁱ	263	Thiamine pyrophosphate3 Publications	1
Siteⁱ	263	Important for catalytic activity	1
Binding siteⁱ	359	Substrate	1
Binding siteⁱ	386	Substrate	1
Active siteⁱ	418	Proton donorCurated	1
Binding siteⁱ	418	Thiamine pyrophosphate3 Publications	1
Binding siteⁱ	445	Thiamine pyrophosphate3 Publications	1
Binding siteⁱ	469	Substrate	1
Binding siteⁱ	477	Substrate	1
Binding siteⁱ	528	Substrate	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	116 – 118	Thiamine pyrophosphate3 Publications		3

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

pentose-phosphate shunt
Source: SGD
Inferred from mutant phenotypeⁱ
- "Pentose-phosphate pathway in Saccharomyces cerevisiae: analysis of deletion mutants for transketolase, transaldolase, and glucose 6-phosphate dehydrogenase."
  Schaaff-Gerstenschlager I., Zimmermann F.K.
  Curr Genet 24:373-376(1993) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Ligand	Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAⁱ	2.2.1.1, 984
SABIO-RKⁱ	P23254

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transketolase 1 (EC:2.2.1.1) Short name: TK 1
Gene namesⁱ	Name:TKL1 Ordered Locus Names:YPR074C ORF Names:YP9499.29C
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XVI

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000006278, TKL1
VEuPathDBⁱ	FungiDB:YPR074C

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	30	H → A or Q: Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. 1 Publication	1
Mutagenesisⁱ	30	H → N: Loss of activity. 1 Publication	1
Mutagenesisⁱ	69	H → A: Reduces catalytic activity by about 98%. Decreased affinity for donor substrate. 1 Publication	1
Mutagenesisⁱ	103	H → A or N: Reduces activity by over 96% and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. 2 Publications	1
Mutagenesisⁱ	103	H → F: Loss of activity. 2 Publications	1
Mutagenesisⁱ	162	E → A or Q: Most catalytic properties similar to wild-type. 1 Publication	1
Mutagenesisⁱ	263	H → A: Strongly reduced catalytic activity. 1 Publication	1
Mutagenesisⁱ	359	R → A: Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication	1
Mutagenesisⁱ	382	D → A or R: Severe loss of activity. 1 Publication	1
Mutagenesisⁱ	469	H → A: Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication	1
Mutagenesisⁱ	477	D → A: Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. 1 Publication	1
Mutagenesisⁱ	481	H → A or Q: Reduces catalytic activity by about 95%. 1 Publication	1
Mutagenesisⁱ	528	R → A: Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000191904	2 – 680	Transketolase 1Add BLAST		679

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	286	PhosphoserineCombined sources	1
Modified residueⁱ	335	PhosphoserineCombined sources	1
Modified residueⁱ	402	PhosphoserineCombined sources	1
Modified residueⁱ	492	PhosphoserineCombined sources	1
Cross-linkⁱ	647	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P23254
PaxDbⁱ	P23254
PRIDEⁱ	P23254
TopDownProteomicsⁱ	P23254

2D gel databases

SWISS-2DPAGEⁱ	P23254

SWISS-2DPAGEⁱ

P23254

PTM databases

iPTMnetⁱ	P23254

iPTMnetⁱ

P23254

Interactionⁱ

Subunit structureⁱ

Homodimer.

5 Publications

Manual assertion based on experiment inⁱ

Ref.16
"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.
Ref.17
"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.
Ref.18
"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.
Ref.19
"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.
Ref.20
"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.

Binary interactionsⁱ

Hide details

P23254

With	#Exp.	IntAct
RSP5 [P39940]	2	EBI-19291,EBI-16219
TKL2 [P33315]	3	EBI-19291,EBI-19297

Protein-protein interaction databases

BioGRIDⁱ	36247, 217 interactors
Database of interacting proteins More...DIPⁱ	DIP-6765N
IntActⁱ	P23254, 13 interactors
Molecular INTeraction database More...MINTⁱ	P23254
STRINGⁱ	4932.YPR074C

Miscellaneous databases

RNActⁱ	P23254, protein

RNActⁱ

P23254, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 26	Combined sources	21
Helixⁱ	32 – 46	Combined sources	15
Beta strandⁱ	62 – 67	Combined sources	6
Helixⁱ	68 – 70	Combined sources	3
Helixⁱ	71 – 80	Combined sources	10
Helixⁱ	87 – 90	Combined sources	4
Turnⁱ	91 – 94	Combined sources	4
Helixⁱ	120 – 139	Combined sources	20
Beta strandⁱ	151 – 155	Combined sources	5
Helixⁱ	157 – 161	Combined sources	5
Helixⁱ	163 – 174	Combined sources	12
Beta strandⁱ	180 – 186	Combined sources	7
Beta strandⁱ	188 – 190	Combined sources	3
Beta strandⁱ	191 – 194	Combined sources	4
Helixⁱ	195 – 197	Combined sources	3
Helixⁱ	203 – 210	Combined sources	8
Beta strandⁱ	213 – 218	Combined sources	6
Turnⁱ	220 – 222	Combined sources	3
Helixⁱ	224 – 236	Combined sources	13
Beta strandⁱ	242 – 247	Combined sources	6
Turnⁱ	250 – 253	Combined sources	4
Turnⁱ	255 – 258	Combined sources	4
Helixⁱ	260 – 262	Combined sources	3
Beta strandⁱ	263 – 265	Combined sources	3
Helixⁱ	269 – 278	Combined sources	10
Helixⁱ	291 – 300	Combined sources	10
Helixⁱ	302 – 322	Combined sources	21
Helixⁱ	324 – 334	Combined sources	11
Helixⁱ	342 – 345	Combined sources	4
Helixⁱ	358 – 369	Combined sources	12
Turnⁱ	370 – 372	Combined sources	3
Beta strandⁱ	376 – 382	Combined sources	7
Helixⁱ	384 – 387	Combined sources	4
Beta strandⁱ	402 – 406	Combined sources	5
Beta strandⁱ	411 – 413	Combined sources	3
Helixⁱ	418 – 431	Combined sources	14
Beta strandⁱ	436 – 442	Combined sources	7
Helixⁱ	443 – 446	Combined sources	4
Helixⁱ	447 – 449	Combined sources	3
Helixⁱ	450 – 459	Combined sources	10
Beta strandⁱ	464 – 468	Combined sources	5
Helixⁱ	472 – 474	Combined sources	3
Turnⁱ	479 – 481	Combined sources	3
Helixⁱ	486 – 491	Combined sources	6
Beta strandⁱ	493 – 495	Combined sources	3
Beta strandⁱ	497 – 499	Combined sources	3
Helixⁱ	504 – 516	Combined sources	13
Beta strandⁱ	522 – 525	Combined sources	4
Beta strandⁱ	528 – 531	Combined sources	4
Helixⁱ	539 – 542	Combined sources	4
Beta strandⁱ	547 – 550	Combined sources	4
Beta strandⁱ	556 – 561	Combined sources	6
Helixⁱ	565 – 577	Combined sources	13
Turnⁱ	578 – 580	Combined sources	3
Beta strandⁱ	583 – 587	Combined sources	5
Helixⁱ	591 – 596	Combined sources	6
Helixⁱ	599 – 605	Combined sources	7
Beta strandⁱ	608 – 610	Combined sources	3
Beta strandⁱ	612 – 615	Combined sources	4
Helixⁱ	623 – 625	Combined sources	3
Beta strandⁱ	628 – 631	Combined sources	4
Helixⁱ	642 – 648	Combined sources	7
Helixⁱ	653 – 667	Combined sources	15

Show more details

3D structure databases

SMRⁱ	P23254
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P23254

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0523, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000176704
HOGENOMⁱ	CLU_009227_0_0_1
InParanoidⁱ	P23254
OMAⁱ	GCAPMGY

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02012, TPP_TK, 1 hit
Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N
PANTHERⁱ	PTHR43522, PTHR43522, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit
SMARTⁱ	View protein in SMART SM00861, Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit
TIGRFAMsⁱ	TIGR00232, tktlase_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P23254-1 [UniParc]FASTA Add to basket

« Hide

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

Length:680

Mass (Da):73,806

Last modified:January 23, 2007 - v4

Checksum:ⁱ40225EAA23A63835

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	37 – 38	MA → RS in AAA35168 (PubMed:1737042).Curated	2
Sequence conflictⁱ	45 – 77	WSQMR…LLYSM → GESNAHEPNQPKTGSTEIDL SCLTVTRSLCCIY in AAA35168 (PubMed:1737042).CuratedAdd BLAST	33
Sequence conflictⁱ	136 – 143	AATYNKPG → DMPLTTSRA in AAA35168 (PubMed:1737042).Curated	8
Sequence conflictⁱ	232 – 234	AQA → RQR in AAA35168 (PubMed:1737042).Curated	3
Sequence conflictⁱ	243 – 257	LIKMT…GSLHA → FDQNDHNHWLRFLRS AA sequence (PubMed:1737042).CuratedAdd BLAST	15
Sequence conflictⁱ	383	L → LVLPIL AA sequence (PubMed:1737042).Curated	1
Sequence conflictⁱ	396	D → S in AAA35168 (PubMed:1737042).Curated	1
Sequence conflictⁱ	528 – 538	RQNLPQLEGSS → PDKTCHNWKVAL in AAA35168 (PubMed:1737042).CuratedAdd BLAST	11
Sequence conflictⁱ	639 – 680	SGKAP…LKKAF → PVRHQKSSSSSVSPQKVLLK ELKRPLHSIRVTS in AAA35168 (PubMed:1737042).CuratedAdd BLAST	42

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	A49510, XJBYTK
NCBI Reference Sequences More...RefSeqⁱ	NP_015399.1, NM_001184171.1

Genome annotation databases

EnsemblFungiⁱ	YPR074C_mRNA; YPR074C; YPR074C
GeneIDⁱ	856188
KEGGⁱ	sce:YPR074C

Protein	Similar proteins		Species	Score	Length	Source
P23254	Transketolase		YEASX		680	UniRef100_P23254
Transketolase		Saccharomyces boulardii (nom. inval.)		680
Transketolase		YEASK		680
Transketolase		YEASC		680
Transketolase		SACPS		680
+3

Protein	Similar proteins		Species	Score	Length	Source
P23254	Transketolase		YEASX		680	UniRef90_P23254
Transketolase		Saccharomyces boulardii (nom. inval.)		680
Transketolase		YEASK		680
Transketolase		YEASC		680
Transketolase		SACPS		680
+12

Protein	Similar proteins		Species	Score	Length	Source
P23254	Transketolase		KLULA		679	UniRef50_P23254
Transketolase	)	PICST		677
Probable transketolase		SCHPO		685
Transketolase 1		CANAX		677
Transketolase		YEASX		680
+242

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	A49510, XJBYTK
RefSeqⁱ	NP_015399.1, NM_001184171.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	1-680	[»]
	1TKA	X-ray	2.70	A/B	3-680	[»]
	1TKB	X-ray	2.30	A/B	3-680	[»]
	1TKC	X-ray	2.70	A/B	3-680	[»]
	1TRK	X-ray	2.00	A/B	1-680	[»]
SMRⁱ	P23254
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	36247, 217 interactors
DIPⁱ	DIP-6765N
IntActⁱ	P23254, 13 interactors
MINTⁱ	P23254
STRINGⁱ	4932.YPR074C

PTM databases

iPTMnetⁱ	P23254

iPTMnetⁱ

P23254

2D gel databases

SWISS-2DPAGEⁱ	P23254

SWISS-2DPAGEⁱ

P23254

Proteomic databases

MaxQBⁱ	P23254
PaxDbⁱ	P23254
PRIDEⁱ	P23254
TopDownProteomicsⁱ	P23254

Genome annotation databases

EnsemblFungiⁱ	YPR074C_mRNA; YPR074C; YPR074C
GeneIDⁱ	856188
KEGGⁱ	sce:YPR074C

Organism-specific databases

SGDⁱ	S000006278, TKL1
VEuPathDBⁱ	FungiDB:YPR074C

Phylogenomic databases

eggNOGⁱ	KOG0523, Eukaryota
GeneTreeⁱ	ENSGT00940000176704
HOGENOMⁱ	CLU_009227_0_0_1
InParanoidⁱ	P23254
OMAⁱ	GCAPMGY

Enzyme and pathway databases

BRENDAⁱ	2.2.1.1, 984
SABIO-RKⁱ	P23254

Miscellaneous databases

EvolutionaryTraceⁱ	P23254
Protein Ontology More...PROⁱ	PR:P23254
RNActⁱ	P23254, protein

Family and domain databases

CDDⁱ	cd02012, TPP_TK, 1 hit
Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N
PANTHERⁱ	PTHR43522, PTHR43522, 1 hit
Pfamⁱ	View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit
SMARTⁱ	View protein in SMART SM00861, Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit
TIGRFAMsⁱ	TIGR00232, tktlase_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TKT1_YEAST
Accessionⁱ	P23254Primary (citable) accession number: P23254 Secondary accession number(s): D6W478
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
	Last sequence update:	January 23, 2007
	Last modified:	February 10, 2021
	This is version 208 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Yeast chromosome XVI
Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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UniProtKB - P23254 (TKT1_YEAST)

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Transketolase 1

TKL1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P23254

Protein-protein interaction databases

Miscellaneous databases

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Miscellaneous databases

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Functionⁱ

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GO - Molecular functionⁱ

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Pathology & Biotechⁱ

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Keywords - PTMⁱ

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Cross-referencesⁱ

Entry informationⁱ

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Keywords - Technical termⁱ