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P34214

- TAL1_KLULA

UniProt

P34214 - TAL1_KLULA

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Protein
Transaldolase
Gene
TAL1, KLLA0A02607g
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.UniRule annotation

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431Schiff-base intermediate with substrate By similarity

GO - Molecular functioni

  1. sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. pentose-phosphate shunt Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pentose shunt

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

UniPathwayiUPA00115; UER00414.

Names & Taxonomyi

Protein namesi
Recommended name:
Transaldolase (EC:2.2.1.2)
Gene namesi
Name:TAL1
Ordered Locus Names:KLLA0A02607g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome A

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 334333TransaldolaseUniRule annotation
PRO_0000173570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP34214.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi28985.P34214.

Structurei

3D structure databases

ProteinModelPortaliP34214.
SMRiP34214. Positions 12-332.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0176.
HOGENOMiHOG000281234.
KOiK00616.
OMAiSYEPHED.
OrthoDBiEOG7N905G.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P34214-1 [UniParc]FASTAAdd to Basket

« Hide

MSEPSAKKQK FANSLEALKA TGTTVVADTG DFESIAKFTP QDATTNPSLI    50
LAAAKQQAYA KLIDSAVQYG KKQGQNIDEQ VEIAVDKLLV EFGTAILKVV 100
PGRVSTEVDA RLSFDKDATV KKALEIIKLY EAEGISKDRV LIKIASTWEG 150
IQAAQELEKE HDIHVNLTLL FSFAQAVAAA EANVTLISPF VGRILDWYKA 200
STGETYTAET DPGVISVKSI YNYYKKHGYN TIVMGASFRN VGEIKALAGV 250
DFLTISPKLL DELLSSDEPV AKILDPESAK AEGSERVSFI NDEPKFRFEL 300
NEDAMATEKL SEGIRKFSAD IVTLFDLIKA KIQA 334
Length:334
Mass (Da):36,477
Last modified:January 23, 2007 - v3
Checksum:iDD67646509EE7099
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z17317 Genomic DNA. Translation: CAA78965.1.
CR382121 Genomic DNA. Translation: CAH02703.1.
PIRiS39870.
RefSeqiXP_451115.1. XM_451115.1.

Genome annotation databases

GeneIDi2896669.
KEGGikla:KLLA0A02607g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z17317 Genomic DNA. Translation: CAA78965.1 .
CR382121 Genomic DNA. Translation: CAH02703.1 .
PIRi S39870.
RefSeqi XP_451115.1. XM_451115.1.

3D structure databases

ProteinModelPortali P34214.
SMRi P34214. Positions 12-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 28985.P34214.

Proteomic databases

PRIDEi P34214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2896669.
KEGGi kla:KLLA0A02607g.

Phylogenomic databases

eggNOGi COG0176.
HOGENOMi HOG000281234.
KOi K00616.
OMAi SYEPHED.
OrthoDBi EOG7N905G.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00414 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00492. Transaldolase_1.
InterProi IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view ]
PANTHERi PTHR10683. PTHR10683. 1 hit.
Pfami PF00923. Transaldolase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00874. talAB. 1 hit.
PROSITEi PS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTAL1_KLULA
AccessioniPrimary (citable) accession number: P34214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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