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

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Cross-references

Sequence databases

EMBL

X60347; CAA42905.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18483; DEJMG.

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

ModBase

P26518.

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.

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`	`1 341`	`341`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145604`
`NP_BIND`	`15 16`	`2`	`NAD (By similarity).`
`REGION`	`155 157`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`215 216`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`156 156`		`Nucleophile (By similarity).`
`BINDING`	`37 37`		`NAD (By similarity).`
`BINDING`	`84 84`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`186 186`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`238 238`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`320 320`		`NAD (By similarity).`
`SITE`	`183 183`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

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

Molecular weight: 36982 Da [This is the MW of the unprocessed precursor]

CRC64: DA1B98CDB9BE2F51 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGGKKIKIGI NGFGRIGRLV ARVALQRDDV ELVAVNDPFI TTDYMTYMFK YDSVHGQWKH 

        70         80         90        100        110        120 
HELKVKDSKT LLFGEKPVTV FGVRNPEEIP WGETGAEFVV ESTGVFTDKD KAAAHLKGGA 

       130        140        150        160        170        180 
KKVIISAPSK DAPMFVVGVN EHEYKSNIDI VSNASCTTNC LAPLAKVIND KFGIVEGLMT 

       190        200        210        220        230        240 
TVHSITATQK TVDGPSSKDW RGGRAAGFNI IPSSTGAAKA VGKVLPALNG KLTGMAFRVP 

       250        260        270        280        290        300 
TVDVSVVDLT VRLEKAASYE EIKAVIKAES EGKLKGILGY TEEDVVSTDF IGDNRSSIFD 

       310        320        330        340 
AKAGIALNEH FVKLVSWYDN EWGYSSRVID LILIVHMASC Q

P26518 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