[1]	NUCLEOTIDE SEQUENCE. DOI=10.1007/BF02602911; PubMed=2515291 [NCBI, ExPASy, EBI, Israel, Japan] Quigley F., Brinkmann H., Martin W.F., Cerff R.; "Strong functional GC pressure in a light-regulated maize gene encoding subunit GAPA of chloroplast glyceraldehyde-3-phosphate dehydrogenase: implications for the evolution of GAPA pseudogenes."; J. Mol. Evol. 29:412-421(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3357887 [NCBI, ExPASy, EBI, Israel, Japan] Quigley F., Martin W.F., Cerff R.; "Intron conservation across the prokaryote-eukaryote boundary: structure of the nuclear gene for chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize."; Proc. Natl. Acad. Sci. U.S.A. 85:2672-2676(1988).
[3]	NUCLEOTIDE SEQUENCE OF 1-125 AND 301-403. STRAIN=cv. W64 X W128E; TISSUE=Leaf; PubMed=16666879 [NCBI, ExPASy, EBI, Israel, Japan] Gowri G., Campbell W.H.; "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase."; Plant Physiol. 90:792-798(1989).

Comments

CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NADP⁺ = 3-phospho-D-glyceroyl phosphate + NADPH.
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B chains (GAPDH 1) (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

X15408; CAA33455.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18976; AAA33464.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31481; AAA33484.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31483; AAA33485.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A30890; DEZMG3.

NP_001105414.1; -.

3D structure databases

HSSP

P19866; 1NBO. [HSSP ENTRY / PDB]

SMR

P09315; 67-403.

ModBase

P09315.

Organism-specific databases

Gramene

P09315; -.

MaizeGDB

13872; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0047100;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity (inferred from electronic annotation from EC).
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:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (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

542368; -.

Other

ProtoNet

P09315.

UniRef

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

Keywords

Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 66`	`66`	`Chloroplast.`
`CHAIN`	`67 403`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic.`	`PRO_0000010422`
`NP_BIND`	`77 78`	`2`	`NADP (By similarity).`
`REGION`	`219 221`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`278 279`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`220 220`		`Nucleophile (By similarity).`
`BINDING`	`102 102`		`NADP (By similarity).`
`BINDING`	`147 147`		`NADP; via carbonyl oxygen (By similarity).`
`BINDING`	`250 250`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`265 265`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`301 301`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`383 383`		`NADP (By similarity).`
`SITE`	`247 247`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 42867 Da [This is the MW of the unprocessed precursor]

CRC64: 0505124C3F458DD8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASSMLSATT VPLQQGGGLS EFSGLRSSAS LPMRRNATSD DFMSAVSFRT HAVGTSGGPR 

        70         80         90        100        110        120 
RAPTEAKLKV AINGFGRIGR NFLRCWHGRG DASPLDVIAI NDTGGVKQAS HLLKYDSTLG 

       130        140        150        160        170        180 
IFDADVKPVG DNAISVDGKV IKVVSDRNPS NLPWGELGID LVIEGTGVFV DREGAGKHIQ 

       190        200        210        220        230        240 
AGAKKVLITA PGKGDIPTYV VGVNADQYNP DEPIISNASC TTNCLAPFVK VLDQKFGIIK 

       250        260        270        280        290        300 
GTMTTTHSYT GDQRLLDASH RDLRRARAAA LNIVPTSTGA AKAVSLVLPN LKGKLNGIAL 

       310        320        330        340        350        360 
RVPTPNVSVV DLVVQVSKKT LAEEVNQAFR DAAANELTGI LEVCDVPLVS VDFRCSDVSS 

       370        380        390        400 
TIDASLTMVM GDDMVKVISW YDNEWGYSQR VVDLADICAN QWK

P09315 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