[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Norway; DOI=10.1007/BF00312639; PubMed=7916671 [NCBI, ExPASy, EBI, Israel, Japan] Zhou Y.H., Ragan M.A.; "cDNA cloning and characterization of the nuclear gene encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa."; Curr. Genet. 23:483-489(1993).
[2]	SEQUENCE REVISION. DOI=10.1007/BF00326308; PubMed=7954900 [NCBI, ExPASy, EBI, Israel, Japan] Zhou Y.H., Ragan M.A.; "Cloning and characterization of the nuclear gene encoding plastid glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa."; Curr. Genet. 26:79-86(1994).

Comments

CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NADP⁺ = 3-phospho-D-glyceroyl phosphate + NADPH.
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

Z15102; CAA78811.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L22011; AAA33355.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S45484; S45484.

3D structure databases

HSSP

P19866; 1NBO. [HSSP ENTRY / PDB]

ModBase

P30724.

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.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PS00071; GAPDH; 1.

Other

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 78`	`78`	`Chloroplast (Potential).`
`CHAIN`	`79 416`	`338`	`Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic.`	`PRO_0000010420`
`NP_BIND`	`90 91`	`2`	`NADP (By similarity).`
`REGION`	`232 234`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`291 292`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`233 233`		`Nucleophile (By similarity).`
`BINDING`	`114 114`		`NADP (By similarity).`
`BINDING`	`158 158`		`NADP; via carbonyl oxygen (By similarity).`
`BINDING`	`263 263`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`278 278`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`314 314`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`396 396`		`NADP (By similarity).`
`SITE`	`260 260`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 416 AA [This is the length of the unprocessed precursor]

Molecular weight: 44338 Da [This is the MW of the unprocessed precursor]

CRC64: 33B9437E84230BD8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFVAPVSSV FSTSSKSAVC SGRSSFAQFS GLKKVNNTAR LQTAEQGSAF GGVSDANDAF 

        70         80         90        100        110        120 
FNAVNTMGAP ARTSNAPSMK VRVAINGFGR IGRNFIRCWA GRTDSNMDVV CINDTSGVKT 

       130        140        150        160        170        180 
ASHLLKYDSI LGTFDSDVVA GEDSITVDGK TIKVVSNRNP LELPWKEMEI DIVVEATGVF 

       190        200        210        220        230        240 
VDAVGAGKHI QAGAKKVLIT APGKGEGVGT FVVGVNDHLY SHDKFDIVSN ASCTTNCMAP 

       250        260        270        280        290        300 
FMKVLDDEFG VVRGMMTTTH SYTGDQRLLD AGHRDLRRAR SAALNIVPTT TGAAKAVALV 

       310        320        330        340        350        360 
VPTLAGKLNG IALRVPTPNV SVCDVVMQVS KKTFKEEVNG ALLKAANGSM KGIIKYSDEP 

       370        380        390        400        410 
LVSCDYRGTD ESTIIDSSLT MVMGDDMLKV VAWYDNEWGY SQRVVDLGEV MASQWK

P30724 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