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Reviewed, UniProtKB/Swiss-Prot P25861 (G3PC_ANTMA)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
    EC=1.2.1.12
Gene names
Name: GAPC
Synonyms: GAPDH
OrganismAntirrhinum majus (Garden snapdragon)
Taxonomic identifier4151 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Plantaginaceae › Antirrhineae › Antirrhinum

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Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Miscellaneous

Plants contain three forms of GAPDH: a cytosolic form which participates in glycolysis and two chloroplast forms which participates in photosynthesis. These three forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) 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 – 337337Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145593

Regions

Nucleotide binding13 – 142NAD By similarity
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region213 – 2142Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site351NAD By similarity
Binding site821NAD; via carbonyl oxygen By similarity
Binding site1841Glyceraldehyde 3-phosphate By similarity
Binding site2361Glyceraldehyde 3-phosphate By similarity
Binding site3181NAD By similarity
Site1811Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P25861-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0E0E69F1F474F0D7

FASTA33736,685
        10         20         30         40         50         60 
MAPIKIGING FGRIGRLVAR VALQRDDVEL VAVNDPFIST DYMTYMFKYD SVHGAWKHHE 

        70         80         90        100        110        120 
LKVKDEKTLL FGEKPVVVFG RRNPEEIPRA STGAEYIVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VIISAPSKDA PMFVVGVNEK EYKSDLHIVS NASCTTNCLA PLAKVINDRF GIVEGLMTTV 

       190        200        210        220        230        240 
HSITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPQLNGKL TGMSFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVR LEKKATYEQI KAAIKEESEG KLKGILGYTE DDVVSTDFVG DSRSSIFDAK 

       310        320        330 
AGIALNDNFV KLVSWYDNEW GYSTRVVDLI VHMASVQ

« Hide

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References

[1]"Molecular evidence for pre-Cretaceous angiosperm origins."
Martin W., Gierl A., Seadler H.
Nature 339:46-48(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

X59517 mRNA. Translation: CAA42103.1. Different initiation.
PIRDESKG. S17991.

3D structure databases

HSSPHSSP built from PDB template 1IHX based on UniProtKB P56649.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 189180.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3PC_ANTMA
AccessionPrimary (citable) accession number: P25861
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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