Reviewed, UniProtKB/Swiss-Prot P34214 (TAL1_KLULA)

Names and origin

Protein names

Recommended name:
    Transaldolase
    EC=2.2.1.2

Gene names

Name:	TAL1
Ordered Locus Names:	KLLA0A02607g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

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

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.
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-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	transaldolase 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)
	P34214-1 [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: 7934848] [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: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z17317 Genomic DNA. Translation: CAA78965.1. CR382121 Genomic DNA. Translation: CAH02703.1.
PIR	S39870.
RefSeq	XP_451115.1.
3D structure databases
HSSP	HSSP built from PDB template 1F05 based on UniProtKB P37837.
ModBase	Search...
Protein-protein interaction databases
STRING	P34214.
Genome annotation databases
GeneID	2896669.
GenomeReviews	Gene locus KLLA0A02607g in contig CR382121_GR.
KEGG	kla:KLLA0A02607g.
Phylogenomic databases
HOGENOM	P34214.
OMA	GDFEAMR.
Enzyme and pathway databases
BRENDA	2.2.1.2. 74088.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_AB. IPR018225. Transaldolase_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR10683. Transaldolase. 1 hit. PTHR10683:SF3. Transaldolase_AB. 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:	November 3, 2009
This is version 65 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)