P34214 (TAL1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Gene names

Name:	TAL1
Ordered Locus Names:	KLLA0A02607g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity.
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Molecular function	Transferase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 334	333	Transaldolase		PRO_0000173570
Sites
	Active site	143	1	By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34214 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DD67646509EE7099	FASTA	334	36,477
	10 20 30 40 50 60 MSEPSAKKQK FANSLEALKA TGTTVVADTG DFESIAKFTP QDATTNPSLI LAAAKQQAYA 70 80 90 100 110 120 KLIDSAVQYG KKQGQNIDEQ VEIAVDKLLV EFGTAILKVV PGRVSTEVDA RLSFDKDATV 130 140 150 160 170 180 KKALEIIKLY EAEGISKDRV LIKIASTWEG IQAAQELEKE HDIHVNLTLL FSFAQAVAAA 190 200 210 220 230 240 EANVTLISPF VGRILDWYKA STGETYTAET DPGVISVKSI YNYYKKHGYN TIVMGASFRN 250 260 270 280 290 300 VGEIKALAGV DFLTISPKLL DELLSSDEPV AKILDPESAK AEGSERVSFI NDEPKFRFEL 310 320 330 NEDAMATEKL SEGIRKFSAD IVTLFDLIKA KIQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway." Jacoby J., Hollenberg C.P., Heinisch J.J. Mol. Microbiol. 10:867-876(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z17317 Genomic DNA. Translation: CAA78965.1. CR382121 Genomic DNA. Translation: CAH02703.1.
PIR	S39870.
RefSeq	XP_451115.1. XM_451115.1.
3D structure databases
ProteinModelPortal	P34214.
SMR	P34214. Positions 12-332.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.P34214.
Proteomic databases
PRIDE	P34214.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2896669.
KEGG	kla:KLLA0A02607g.
Phylogenomic databases
eggNOG	COG0176.
HOGENOM	HOG000281234.
KO	K00616.
OMA	RYQTVIM.
OrthoDB	EOG4XWK6K.
Enzyme and pathway databases
UniPathway	UPA00115; UER00414.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_1. IPR018225. Transaldolase_AS. [Graphical view]
PANTHER	PTHR10683. PTHR10683. 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...

Entry information

Entry name

TAL1_KLULA

Accession

Primary (citable) accession number: P34214

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program