[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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).

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

L07501; AAA33779.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09663; T09663.

3D structure databases

HSSP

P00357; 4GPD. [HSSP ENTRY / PDB]

ModBase

P34924.

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`	`1 340`	`340`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145614`
`NP_BIND`	`16 17`	`2`	`NAD (By similarity).`
`REGION`	`156 158`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`216 217`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`157 157`		`Nucleophile (By similarity).`
`BINDING`	`38 38`		`NAD (By similarity).`
`BINDING`	`85 85`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`187 187`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`239 239`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`321 321`		`NAD (By similarity).`
`SITE`	`184 184`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 340 AA [This is the length of the unprocessed precursor]

Molecular weight: 36530 Da [This is the MW of the unprocessed precursor]

CRC64: 1E81ACA460086F01 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSTGKIKIG INGFGRIGRL VARVALTRDD IELVGVNDPF ISTDYMSYMF KYDSVHGKWK 

        70         80         90        100        110        120 
HHEVNVKDSK TLLFGEKSVA VFGCRNPEEI PWGEVGAEYV VESTGVFTDK EKASAHLKAG 

       130        140        150        160        170        180 
AKKVVISAPS KDAPMFVVGV NEHQYKSDVN IVSNASCTTN CLAPLAKVIN DKFGIVEGLM 

       190        200        210        220        230        240 
TTVHSITATQ KTVDGPSNKD WRGGRGAGFN IIPSSTGAAK AVGKVLPALN GKLTGMAFRV 

       250        260        270        280        290        300 
PTPDVSVVDL TVRLEKSATY DEIKAAIKAE SEGNLKGILG YTEDAVVSTD FIGDSRSSIF 

       310        320        330        340 
DAQAGIALSD NFVKLVSWYD NEWGYSSRVV DLIVHMAATQ

P34924 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