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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Columba livia (Rock dove)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins (By similarity).By similarity

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
  2. Phosphoglycerate kinase (PGK1)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase (A306_12207), Pyruvate kinase (A306_00006759)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33NADBy similarity1
Binding sitei78NAD; via carbonyl oxygenBy similarity1
Active sitei150NucleophilePROSITE-ProRule annotation1
Sitei177Activates thiol group during catalysisBy similarity1
Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
Binding sitei232Glyceraldehyde 3-phosphateBy similarity1
Binding sitei314NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 12NADBy similarity2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase, Transferase
Biological processApoptosis, Glycolysis
LigandNAD

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00184

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
Gene namesi
Name:GAPDH
Synonyms:GAPD
OrganismiColumba livia (Rock dove)
Taxonomic identifieri8932 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeColumbiformesColumbidaeColumba

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001454972 – 333Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei150S-nitrosocysteineBy similarity1

Post-translational modificationi

S-nitrosylation of Cys-150 leads to translocation to the nucleus.By similarity

Keywords - PTMi

S-nitrosylation

Proteomic databases

PRIDEiO57479

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliO57479
SMRiO57479
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 151Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni209 – 210Glyceraldehyde 3-phosphate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000227
KOiK00134

Family and domain databases

InterProiView protein in InterPro
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR006424 Glyceraldehyde-3-P_DH_1
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR10836 PTHR10836, 1 hit
PfamiView protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit
PIRSFiPIRSF000149 GAP_DH, 1 hit
PRINTSiPR00078 G3PDHDRGNASE
SMARTiView protein in SMART
SM00846 Gp_dh_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
PROSITEiView protein in PROSITE
PS00071 GAPDH, 1 hit

Sequencei

Sequence statusi: Complete.

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

O57479-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA ILSAKVQVVA INDPFIDLNY MVYMFKYDST
60 70 80 90 100
HGHFRGTVKA ENGKLVINGN AITIFQERDP SNIKWADAGA EYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDK SLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
260 270 280 290 300
AKYDDIKRVV KAAADGPLKG ILAYTEDQVV SCDFNGDSHS STFDAGAGIA
310 320 330
LNDHFVKLVS WYDNEYGYSN RVVDLMVHMA SKE
Length:333
Mass (Da):35,767
Last modified:January 23, 2007 - v3
Checksum:i8C84ADDD181E33AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036934 mRNA Translation: AAB88869.1
RefSeqiNP_001269764.1, NM_001282835.1

Genome annotation databases

GeneIDi102089934
KEGGiclv:102089934

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036934 mRNA Translation: AAB88869.1
RefSeqiNP_001269764.1, NM_001282835.1

3D structure databases

ProteinModelPortaliO57479
SMRiO57479
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO57479

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102089934
KEGGiclv:102089934

Organism-specific databases

CTDi2597

Phylogenomic databases

HOVERGENiHBG000227
KOiK00134

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00184

Family and domain databases

InterProiView protein in InterPro
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR006424 Glyceraldehyde-3-P_DH_1
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR10836 PTHR10836, 1 hit
PfamiView protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit
PIRSFiPIRSF000149 GAP_DH, 1 hit
PRINTSiPR00078 G3PDHDRGNASE
SMARTiView protein in SMART
SM00846 Gp_dh_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
PROSITEiView protein in PROSITE
PS00071 GAPDH, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiG3P_COLLI
AccessioniPrimary (citable) accession number: O57479
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 93 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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