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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gapdh

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 annotationBy similarity

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.By similarity
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gapdhs), Glyceraldehyde-3-phosphate dehydrogenase 2 (gapdh-2), Glyceraldehyde-3-phosphate dehydrogenase (gapdh), Glyceraldehyde-3-phosphate dehydrogenase (gapdh)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase 4 (eno4)
  5. Pyruvate kinase, Pyruvate kinase, Pyruvate kinase, Pyruvate kinase (pkmb), Pyruvate kinase, Pyruvate kinase (pkma), Pyruvate kinase (pkma), Pyruvate kinase (pklr), Pyruvate kinase (pklr), Pyruvate kinase (pkmb), Pyruvate kinase (pkma)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NADBy similarity
Binding sitei78 – 781NAD; via carbonyl oxygenBy similarity
Active sitei150 – 1501NucleophilePROSITE-ProRule annotationBy similarity
Sitei177 – 1771Activates thiol group during catalysisBy similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
Binding sitei314 – 3141NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-DRE-70171. Glycolysis.
R-DRE-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenaseBy similarity (EC:1.2.1.12)
Short name:
GAPDHBy similarity
Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
Gene namesi
Name:gapdhImported
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 16

Organism-specific databases

ZFINiZDB-GENE-030115-1. gapdh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Glyceraldehyde-3-phosphate dehydrogenasePRO_0000382469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501S-nitrosocysteineBy similarity

Post-translational modificationi

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

Keywords - PTMi

S-nitrosylation

Proteomic databases

PaxDbiQ5XJ10.
PRIDEiQ5XJ10.

Expressioni

Gene expression databases

BgeeiQ5XJ10.
ExpressionAtlasiQ5XJ10. differential.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000063799.

Structurei

3D structure databases

ProteinModelPortaliQ5XJ10.
SMRiQ5XJ10. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.Sequence analysis

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiQ5XJ10.
KOiK00134.
OrthoDBiEOG7Q5HDF.
PhylomeDBiQ5XJ10.
TreeFamiTF300533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XJ10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKVGINGFG RIGRLVTRAA FLTKKVEIVA INDPFIDLDY MVYMFQYDST
60 70 80 90 100
HGKYKGEVKA EGGKLVIDGH AITVYSERDP ANIKWGDAGA TYVVESTGVF
110 120 130 140 150
TTIEKASAHI KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLTVVSNASC
160 170 180 190 200
TTNCLAPLAK VINDNFVIVE GLMSTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
SQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTVRLEKP
260 270 280 290 300
AKYDEIKKVV KAAADGPMKG ILGYTEHQVV STDFNGDCRS SIFDAGAGIA
310 320 330
LNDHFVKLVT WYDNEFGYSN RVCDLMAHMA SKE
Length:333
Mass (Da):35,784
Last modified:September 19, 2006 - v2
Checksum:i206FC71AA4774526
GO

Sequence cautioni

The sequence AAI15132.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101G → E in AAI15132 (Ref. 1) Curated
Sequence conflicti318 – 3181Y → H in AAI15132 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083506 mRNA. Translation: AAH83506.2.
BC095386 mRNA. Translation: AAH95386.2.
BC115131 mRNA. Translation: AAI15132.1. Different initiation.
RefSeqiNP_001108586.1. NM_001115114.1.
UniGeneiDr.35640.

Genome annotation databases

EnsembliENSDART00000063800; ENSDARP00000063799; ENSDARG00000043457.
GeneIDi317743.
KEGGidre:317743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083506 mRNA. Translation: AAH83506.2.
BC095386 mRNA. Translation: AAH95386.2.
BC115131 mRNA. Translation: AAI15132.1. Different initiation.
RefSeqiNP_001108586.1. NM_001115114.1.
UniGeneiDr.35640.

3D structure databases

ProteinModelPortaliQ5XJ10.
SMRiQ5XJ10. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000063799.

Proteomic databases

PaxDbiQ5XJ10.
PRIDEiQ5XJ10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000063800; ENSDARP00000063799; ENSDARG00000043457.
GeneIDi317743.
KEGGidre:317743.

Organism-specific databases

CTDi2597.
ZFINiZDB-GENE-030115-1. gapdh.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiQ5XJ10.
KOiK00134.
OrthoDBiEOG7Q5HDF.
PhylomeDBiQ5XJ10.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-DRE-70171. Glycolysis.
R-DRE-70263. Gluconeogenesis.

Miscellaneous databases

NextBioi20807170.
PROiQ5XJ10.

Gene expression databases

BgeeiQ5XJ10.
ExpressionAtlasiQ5XJ10. differential.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: EmbryoImported and OvaryImported.

Entry informationi

Entry nameiG3P_DANRE
AccessioniPrimary (citable) accession number: Q5XJ10
Secondary accession number(s): Q1RM54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 19, 2006
Last modified: December 9, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.