[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1016/0022-2836(89)90490-7; PubMed=2716055 [NCBI, ExPASy, EBI, Israel, Japan] Huang X.Y., Barrios L.A.M., Vonkhorporn P., Honda S., Albertson D.G., Hecht R.M.; "Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans."; J. Mol. Biol. 206:411-424(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0167-4781(87)90018-2; PubMed=3026481 [NCBI, ExPASy, EBI, Israel, Japan] Yarbrough P.O., Hayden M.A., Dunn L.A., Vermersch P.S., Klass M.R., Hecht R.M.; "The glyceraldehyde-3-phosphate dehydrogenase gene family in the nematode, Caenorhabditis elegans: isolation and characterization of one of the genes."; Biochim. Biophys. Acta 908:21-33(1987).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).

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: Homotetramer.
INTERACTION:
Q95QC4:zyg-8; NbExp=1; IntAct=EBI-326242, EBI-331795;
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: There are four nearly identical glyceraldehyde 3-phosphate dehydrogenases in C.elegans.
SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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

X52674; CAA36900.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04818; CAA28504.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49070; CAA88870.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S03911; DEKWG1.

NP_496237.1; -.

3D structure databases

HSSP

P56649; 1CRW. [HSSP ENTRY / PDB]

ModBase

P04970.

Protein-protein interaction databases

DIP

DIP:24716N; -.

IntAct

P04970; -.

Organism-specific databases

WormBase

WBGene00001683; gpd-1.

WormPep

T09F3.3; CE02343. [WormPep / WorfDB]

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0008406;	Biological process: gonad development (inferred from mutant phenotype from WormBase).
GO:0002119;	Biological process: nematode larval development (inferred from mutant phenotype from WormBase).
GO:0040018;	Biological process: positive regulation of multicellular organism growth (inferred from mutant phenotype from WormBase).
QuickGo view.

Family and domain databases

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.

PANTHER

PTHR10836; GAP_DH; 1.

Pfam

PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000149; GAP_DH; 1.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PS00071; GAPDH; 1.

Genome annotation databases

Ensembl

T09F3.3; Caenorhabditis elegans. [Contig view]

GeneID

174603; -.

KEGG

cel:T09F3.3; -.

Other

NextBio

884736; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 341`	`341`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000145510`
`NP_BIND`	`13 14`	`2`	`NAD (By similarity).`
`REGION`	`157 159`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`217 218`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`158 158`		`Nucleophile (By similarity).`
`BINDING`	`35 35`		`NAD (By similarity).`
`BINDING`	`85 85`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`188 188`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`240 240`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`322 322`		`NAD (By similarity).`
`SITE`	`185 185`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 36382 Da [This is the MW of the unprocessed precursor]

CRC64: 648E40ED4BD270CC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKANVGING FGRIGRLVLR AAVEKDTVQV VAVNDPFITI DYMVYLFKYD STHGQFKGTV 

        70         80         90        100        110        120 
TYDGDFLIVQ KDGKSSHKIK VFNSKDPAAI AWGSVKADFV VESTGVFTTK EKASAHLQGG 

       130        140        150        160        170        180 
AKKVIISAPS ADAPMYVVGV NHEKYDASND HVVSNASCTT NCLAPLAKVI NDNFGIIEGL 

       190        200        210        220        230        240 
MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR 

       250        260        270        280        290        300 
VPTPDVSVVD LTVRLEKPAS MDDIKKVVKA AADGPMKGIL AYTEDQVVST DFVSDPHSSI 

       310        320        330        340 
FDAGACISLN PNFVKLVSWY DNEYGYSNRV VDLIGYIATR G

P04970 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools