[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Wisconsin 22; DOI=10.1016/0022-2836(89)90147-2; PubMed=2810356 [NCBI, ExPASy, EBI, Israel, Japan] Martinez P., Martin W.F., Cerff R.; "Structure, evolution and anaerobic regulation of a nuclear gene encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from maize."; J. Mol. Biol. 208:551-565(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF02101150; PubMed=3131533 [NCBI, ExPASy, EBI, Israel, Japan] Brinkmann H., Martinez P., Quigley F., Martin W.F., Cerff R.; "Endosymbiotic origin and codon bias of the nuclear gene for chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize."; J. Mol. Evol. 26:320-328(1987).

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

X07156; CAA30151.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15596; CAA33620.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S00354; DEZMGC.

NP_001105413.1; -.

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

ModBase

P08735.

Organism-specific databases

Gramene

P08735; -.

MaizeGDB

13873; -.

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.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PROSITE

PS00071; GAPDH; 1.

Genome annotation databases

GeneID

542367; -.

Other

ProtoNet

P08735.

UniRef

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 1.`	`PRO_0000145605`
`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).`
`CONFLICT`	`336 336`		`T -> S (in Ref. 2; CAA30151).`

Sequence information

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

Molecular weight: 36523 Da [This is the MW of the unprocessed precursor]

CRC64: E18F580F09FDC07B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGKIKIGING FGRIGRLVAR VALQSEDVEL VAVNDPFITT DYMTYMFKYD TVHGHWKHSD 

        70         80         90        100        110        120 
ITLKDSKTLL FGDKPVTVFG IRNPEEIPWG EAGAEYVVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVIHDNF GIVEGLMTTV 

       190        200        210        220        230        240 
HAITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMSFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVR IEKGASYEDI KKAIKAASEG PLKGIMGYVE EDLVSTDFLG DSRSSIFDAK 

       310        320        330 
AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMFKTQ

P08735 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