[1]	NUCLEOTIDE SEQUENCE. PubMed=8095691 [NCBI, ExPASy, EBI, Israel, Japan] Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R.; "Molecular phylogenies in angiosperm evolution."; Mol. Biol. Evol. 10:140-162(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Rosakrone; DOI=10.1038/367387a0; PubMed=8114942 [NCBI, ExPASy, EBI, Israel, Japan] Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.; "Five identical intron positions in ancient duplicated genes of eubacterial origin."; Nature 367:387-389(1994).

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.
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.
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

L07500; AAA33667.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X73150; CAA51675.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T06781; T06781.

3D structure databases

HSSP

P56649; 1CRW. [HSSP ENTRY / PDB]

ModBase

P34922.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProDom

PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PS00071; GAPDH; 1.

Other

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

Keywords

Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 338`	`338`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145610`
`NP_BIND`	`14 15`	`2`	`NAD (By similarity).`
`REGION`	`154 156`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`214 215`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`155 155`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`83 83`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`185 185`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`237 237`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`319 319`		`NAD (By similarity).`
`SITE`	`182 182`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 36609 Da [This is the MW of the unprocessed precursor]

CRC64: 09B55960BE03EA27 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGAKIKIGIN GFGRIGRLVA RVALKRDDVE LVAVNDPFIT TDYMTYMFKY DSVHGQWKND 

        70         80         90        100        110        120 
ELTVKDSNTL LFGQKPVTVF AHRNPEEIPW ASTGADIIVE STGVFTDKDK AAAHLKGGAK 

       130        140        150        160        170        180 
KVIISAPSKD APMFVVGVNE NEYKPEFDII SNASCTTNCL APLAKVINDR FGIVEGLMTT 

       190        200        210        220        230        240 
VHSITATQKT VDGPSSKDWR GGRAASFNII PSSTGAAKAV GKVLPALNGK LTGMSFRVPT 

       250        260        270        280        290        300 
VDVSVVDLTV RLEKAATYDE IKAAIKEESE GKLKGILGYT EDDVVSTDFI GDTRSSIFDA 

       310        320        330 
KAGIALNDKF VKLVSWYDNE LGYSTRVVDL IVHIAKQL

P34922 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