P15019 (TAL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Gene names

Name:	TAL1
Ordered Locus Names:	YLR354C
ORF Names:	L9638.6

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	335 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	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subunit structure	Homodimer.
Miscellaneous	Two isoenzymes seem to be encoded by the same gene. Present with 53000 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay. Source: SGD
Molecular function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARO8	P53090	1	EBI-18952,EBI-2042933
ESS1	P22696	1	EBI-18952,EBI-6679
KAP95	Q06142	1	EBI-18952,EBI-9145
RNR1	P21524	1	EBI-18952,EBI-15234
URN1	Q06525	1	EBI-18952,EBI-35138
YFL010C	P43582	1	EBI-18952,EBI-22766
YJL068C	P40363	1	EBI-18952,EBI-25922

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 335	334	Transaldolase		PRO_0000173574
Sites
	Active site	144	1	Ref.6
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.7
	Modified residue	238	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	221	1	I → M in CAA34078. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15019 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2A3A96D80E22B157	FASTA	335	37,036
	10 20 30 40 50 60 MSEPAQKKQK VANNSLEQLK ASGTVVVADT GDFGSIAKFQ PQDSTTNPSL ILAAAKQPTY 70 80 90 100 110 120 AKLIDVAVEY GKKHGKTTEE QVENAVDRLL VEFGKEILKI VPGRVSTEVD ARLSFDTQAT 130 140 150 160 170 180 IEKARHIIKL FEQEGVSKER VLIKIASTWE GIQAAKELEE KDGIHCNLTL LFSFVQAVAC 190 200 210 220 230 240 AEAQVTLISP FVGRILDWYK SSTGKDYKGE ADPGVISVKK IYNYYKKYGY KTIVMGASFR 250 260 270 280 290 300 STDEIKNLAG VDYLTISPAL LDKLMNSTEP FPRVLDPVSA KKEAGDKISY ISDESKFRFD 310 320 330 LNEDAMATEK LSEGIRKFSA DIVTLFDLIE KKVTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the structural gene for yeast transaldolase." Schaaff I., Hohmann S., Zimmermann F.K. Eur. J. Biochem. 188:597-603(1990) [PubMed: 2185015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204510 / AB320.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The ILV5 gene of Saccharomyces cerevisiae is highly expressed." Petersen J.G.L., Holmberg S. Nucleic Acids Res. 14:9631-9651(1986) [PubMed: 3027658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[5]	Harkins H.A., Pringle J.R. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-335.
[6]	"Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase." Miosga T., Schaaff-Gerstenschlaeger I., Franken E., Zimmermann F.K. Yeast 9:1241-1249(1993) [PubMed: 8109173] [Abstract] Cited for: ACTIVE SITE.
[7]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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-238, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15953 Genomic DNA. Translation: CAA34078.1. U19102 Genomic DNA. Translation: AAB67752.1. X04969 Genomic DNA. Translation: CAA28644.1. L37016 Genomic DNA. Translation: AAA64519.1. BK006945 Genomic DNA. Translation: DAA09658.1.
PIR	S51462.
RefSeq	NP_013458.1. NM_001182243.1.
3D structure databases
ProteinModelPortal	P15019.
SMR	P15019. Positions 12-333.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4980N.
IntAct	P15019. 13 interactions.
MINT	MINT-559744.
STRING	P15019.
2D gel databases
SWISS-2DPAGE	P15019.
Proteomic databases
PeptideAtlas	P15019.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR354C; YLR354C; YLR354C.
GeneID	851068.
KEGG	sce:YLR354C.
NMPDR	fig|4932.3.peg.4480.
Organism-specific databases
SGD	S000004346. TAL1.
Phylogenomic databases
eggNOG	fuNOG07388.
GeneTree	EFGT00050000004933.
HOGENOM	HBG286747.
OMA	DTGDFHA.
OrthoDB	EOG4XWK6K.
Gene expression databases
ArrayExpress	P15019.
Genevestigator	P15019.
GermOnline	YLR354C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_1. IPR018225. Transaldolase_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00616.
PANTHER	PTHR10683. Transaldolase. 1 hit.
Pfam	PF00923. Transaldolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00874. TalAB. 1 hit.
PROSITE	PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967708.

Entry information

Entry name

TAL1_YEAST

Accession

Primary (citable) accession number: P15019
Secondary accession number(s): D6VYZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program