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UniProtKB/Swiss-Prot entry Q8LK61


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GAPN_WHEAT
Primary accession number Q8LK61
Secondary accession number Q8L5J9
Integrated into Swiss-Prot on June 26, 2007
Sequence was last modified on December 20, 2005 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 32)
Name and origin of the protein
Protein name NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Synonyms EC 1.2.1.9
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
Triosephosphate dehydrogenase
Gene name
Name: GAPN
From
Triticum aestivum (Wheat) [TaxID: 4565] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Triticum.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND PHODPHORYLATION.
TISSUE=Endosperm, and Leaf;
DOI=10.1016/S0014-5793(02)03455-5; PubMed=12387887 [NCBI, ExPASy, EBI, Israel, Japan]
Bustos D.M., Iglesias A.A.;
"Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum).";
FEBS Lett. 530:169-173(2002).
[2]
SEQUENCE REVISION.
TISSUE=Leaf;
Piattoni C.V., Guerrero S.A., Bustos D.M., Iglesias A.A.;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH 14-3-3 PROTEIN, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
DOI=10.1104/pp.103.030981; PubMed=14681537 [NCBI, ExPASy, EBI, Israel, Japan]
Bustos D.M., Iglesias A.A.;
"Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins.";
Plant Physiol. 133:2081-2088(2003).
[4]
3D-STRUCTURE MODELING.
DOI=10.1016/j.jmgm.2005.03.002; PubMed=15896993 [NCBI, ExPASy, EBI, Israel, Japan]
Bustos D.M., Iglesias A.A.;
"A model for the interaction between plant GAPN and 14-3-3zeta using protein-protein docking calculations, electrostatic potentials and kinetics.";
J. Mol. Graph. Model. 23:490-502(2005).
Comments
  • FUNCTION: Important as a means of generating NADPH for biosynthetic reactions.
  • CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH.
  • ENZYME REGULATION: Insensitive to magnesium or calcium when dephosphorylated. When phosphorylated, 3-fold activation by magnesium or calcium, 2-fold activation by potasium, inhibited by ADP and AMP and insensitive to ATP or PPi.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=40 µM for NADP;
    KM=118 µM for D-glyceraldehyde-3-phosphate;
    Note=When the protein is phosphorylated, the affinity for substrates is similar but the Vmax is lowered;
  • SUBUNIT: Interacts with 14-3-3 protein when phosphorylated. This interaction is released by divalent cations.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • PTM: Phosphorylated in shoots and non-photosynthetic tissues, but not in leaves.
  • SIMILARITY: Belongs to the aldehyde dehydrogenase family.
  • CAUTION: Sequences of mRNA encoded by the same gene but extracted from leaves (AF521191) or from endosperm (AF521190) differ at several prositions due to sequencing uncertainties.
  • SEQUENCE CAUTION:
    • Sequence=AAM77678.1; Type=Frameshift; Positions=351, 369;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF521190; AAM77678.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF521191; AAM77679.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Ta.47067
3D structure databases
ModBase Q8LK61.
Organism-specific databases
Gramene Q8LK61; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0008886; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
Other
ProtoNet Q8LK61.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   496  496     NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. PRO_0000291765
NP_BIND   245   249  5     NAD (By similarity). 
REGION   169   170  2     Substrate binding (By similarity). 
REGION   297   299  3     Substrate binding (By similarity). 
ACT_SITE   264   264        Proton acceptor (By similarity). 
ACT_SITE   298   298        Nucleophile (By similarity). 
BINDING   116   116        Substrate (By similarity). 
BINDING   192   192        NADP (By similarity). 
BINDING   195   195        NADP (By similarity). 
BINDING   230   230        NADP (By similarity). 
BINDING   391   391        NADP (By similarity). 
BINDING   451   451        Substrate (By similarity). 
SITE   169   169  1     Transition state stabilizer (By similarity). 
MOD_RES   404   404        Phosphoserine (Potential). 
CONFLICT   98    98        S -> C (in Ref. 1; AAM77678). 
CONFLICT   157   157        V -> I (in Ref. 1; AAM77678). 
CONFLICT   172   172        V -> A (in Ref. 1; AAM77678). 
CONFLICT   176   176        V -> G (in Ref. 1; AAM77678). 
CONFLICT   188   188        S -> A (in Ref. 1; AAM77678). 
CONFLICT   316   316        E -> Z (in Ref. 1; AAM77678). 
Sequence information
Length: 496 AA [This is the length of the unprocessed precursor] Molecular weight: 53047 Da [This is the MW of the unprocessed precursor] CRC64: F37AB38E8561A287 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGTGVFADV LDGEVYKYYA DGEWRASASG KTVAIVNPTT RQTQYRVQAC TQEEVNKVMD 

        70         80         90        100        110        120 
AAKVAQKSWA RTPLWKRAEL LHKAAAILKE HKTPIAESLV KEIAKPAKDA VSEVVRSGDL 

       130        140        150        160        170        180 
VSYTAEEGVR ILGEGKLLVS DSFPGNERNK YCLSSKVPLG VVLAIPPFNY PVNLAVSKIG 

       190        200        210        220        230        240 
PALIAGNSLV LKPPTQGAVA ALHMVHCFHL AGFPKGLISC VTGKGSEIGD FLTMHPGVNC 

       250        260        270        280        290        300 
ISFTGGDTGI AISKKAGMVP LQMELGGKDA CIVLEDADLD LVAANIVKGG FSYSGQRCTA 

       310        320        330        340        350        360 
VKVVLIMEAV ADTVVEKVNA KLAKLKVGPP EDDSDITPVV TESSANFIEG LVMDAKEKGA 

       370        380        390        400        410        420 
TFCQEYRREG NLIWPLLLDH VRPDMRIAWE EPFGPVLPVI RINSVEEGIH HCNASNFGLQ 

       430        440        450        460        470        480 
GCVFTRDINK AIMISDAMES GTVQINSAPA RGPDHFPFQG LKDSGIGSQG ITNSINMMTK 

       490 
VKSTVINLPS PSYTMG 

Q8LK61 in FASTA format

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