NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2303458 [NCBI, ExPASy, EBI, Israel, Japan]
Ostrem J.A., Vernon D.M., Bohnert H.J.;
"Increased expression of a gene coding for NAD:glyceraldehyde-3-phosphate dehydrogenase during the transition from C3 photosynthesis to crassulacean acid metabolism in Mesembryanthemum crystallinum.";
J. Biol. Chem. 265:3497-3502(1990).

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

J05223; AAA33033.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29956; AAA33031.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35080; A35080.

3D structure databases

HSSP

P56649; 1IHX. [HSSP ENTRY / PDB]

ModBase

P17878.

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`	`1 337`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145608`
`NP_BIND`	`13 14`	`2`	`NAD (By similarity).`
`REGION`	`1 151`	`151`	`Binding to NAD.`
`REGION`	`152 337`	`186`	`Catalytic.`
`REGION`	`153 155`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`213 214`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`154 154`		`Nucleophile (By similarity).`
`BINDING`	`35 35`		`NAD (By similarity).`
`BINDING`	`82 82`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`184 184`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`236 236`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`318 318`		`NAD (By similarity).`
`SITE`	`181 181`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 36587 Da [This is the MW of the unprocessed precursor]

CRC64: B07B28A25509E9EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKVKVGING FGRIGRLVAR VILQRDDCEL VAVNDPFIST DYMTYMFKYD SVHGQCKSHE 

        70         80         90        100        110        120 
IKLKDEKTLL FGETPVAVFG CRNPEEIPWG QAGADFVVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VVISAPSKDA PMFVVGVNEH EYKSDLNIVS NASCTTNCLA PLAKVINDRF GIVEGLMTTV 

       190        200        210        220        230        240 
HAMTATQKTV DGPSMKDWRG GRAASFNIIP SSTGAAKAVG KVLPALNGKL TGMAFRVPTC 

       250        260        270        280        290        300 
DVSVVDLTVR IEKAASYEQI KAAIKEESEG KLKGILGYTE DDLVSTDFIG DNRSSIFDAK 

       310        320        330 
AGISLNDNFV KLVSWYDNEW GYSTRVVDLI MHISKCQ

P17878 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