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P34214

- TAL1_KLULA

UniProt

P34214 - TAL1_KLULA

Protein

Transaldolase

Gene

TAL1

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
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    Functioni

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

    Catalytic activityi

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

    Pathwayi

    Sites

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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 334333TransaldolasePRO_0000173570Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP34214.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi28985.P34214.

    Structurei

    3D structure databases

    ProteinModelPortaliP34214.
    SMRiP34214. Positions 12-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transaldolase family. Type 1 subfamily.Curated

    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

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    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

    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: October 1, 2014
    This is version 96 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, Reference proteome

    Documents

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

    External Data

    Dasty 3