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Reviewed, UniProtKB/Swiss-Prot Q8LK61 (GAPN_WHEAT)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
    EC=1.2.1.9
Alternative name(s):
    Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
    Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
    Triosephosphate dehydrogenase
Gene names
Name: GAPN
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

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Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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. Ref.3

Subunit structure

Interacts with 14-3-3 protein when phosphorylated. This interaction is released by divalent cations. Ref.3

Subcellular location

Cytoplasm. Ref.3

Post-translational modification

Phosphorylated in shoots and non-photosynthetic tissues, but not in leaves. Ref.1

Sequence similarities

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.

biophysicochemical properties

Kinetic parameters:

When the protein is phosphorylated, the affinity for substrates is similar but the Vmax is lowered.

KM=40 µM for NADP

KM=118 µM for D-glyceraldehyde-3-phosphate

Sequence caution

The sequence AAM77678.1 differs from that shown. Reason: Frameshift at positions 351 and 369.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglyceraldehyde-3-phosphate dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
PRO_0000291765

Regions

Nucleotide binding245 – 2495NAD By similarity
Region169 – 1702Substrate binding By similarity
Region297 – 2993Substrate binding By similarity

Sites

Active site2641Proton acceptor By similarity
Active site2981Nucleophile By similarity
Binding site1161Substrate By similarity
Binding site1921NADP By similarity
Binding site1951NADP By similarity
Binding site2301NADP By similarity
Binding site3911NADP By similarity
Binding site4511Substrate By similarity
Site1691Transition state stabilizer By similarity

Amino acid modifications

Modified residue4041Phosphoserine Potential

Experimental info

Sequence conflict981S → C in AAM77678. Ref.1
Sequence conflict1571V → I in AAM77678. Ref.1
Sequence conflict1721V → A in AAM77678. Ref.1
Sequence conflict1761V → G in AAM77678. Ref.1
Sequence conflict1881S → A in AAM77678. Ref.1
Sequence conflict3161E → Z in AAM77678. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8LK61-1 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: F37AB38E8561A287

FASTA49653,047
        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

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References

[1]"Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)."
Bustos D.M., Iglesias A.A.
FEBS Lett. 530:169-173(2002) [PubMed: 12387887] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION.
Tissue: Endosperm and Leaf.
[2]Piattoni C.V., Guerrero S.A., Bustos D.M., Iglesias A.A.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
Tissue: Leaf.
[3]"Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins."
Bustos D.M., Iglesias A.A.
Plant Physiol. 133:2081-2088(2003) [PubMed: 14681537] [Abstract]
Cited for: INTERACTION WITH 14-3-3 PROTEIN, SUBCELLULAR LOCATION, ENZYME REGULATION.
[4]"A model for the interaction between plant GAPN and 14-3-3zeta using protein-protein docking calculations, electrostatic potentials and kinetics."
Bustos D.M., Iglesias A.A.
J. Mol. Graph. Model. 23:490-502(2005) [PubMed: 15896993] [Abstract]
Cited for: 3D-STRUCTURE MODELING.

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Cross-references

Sequence databases

AF521190 mRNA. Translation: AAM77678.1. Frameshift.
AF521191 mRNA. Translation: AAM77679.2.
UniGeneTa.47067
Ta.511

3D structure databases

ModBaseSearch...

Organism-specific databases

GrameneQ8LK61.

Enzyme and pathway databases

BRENDA1.2.1.9. 253.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGAPN_WHEAT
AccessionPrimary (citable) accession number: Q8LK61
Secondary accession number(s): Q8L5J9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 20, 2005
Last modified: June 16, 2009
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents