NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0092-8674(86)90367-3; PubMed=3757034 [NCBI, ExPASy, EBI, Israel, Japan]
Shih M.-C., Lazar G., Goodman H.M.;
"Evidence in favor of the symbiotic origin of chloroplasts: primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenases.";
Cell 47:73-80(1986).

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

M14417; AAA34075.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24430; A24430.

3D structure databases

HSSP

P19866; 1NBO. [HSSP ENTRY / PDB]

SMR

P09043; 57-392.

ModBase

P09043.

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.

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 56`	`>56`	`Chloroplast.`
`CHAIN`	`57 392`	`336`	`Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic.`	`PRO_0000010427`
`NP_BIND`	`67 68`	`2`	`NADP (By similarity).`
`REGION`	`208 210`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`267 268`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`209 209`		`Nucleophile (By similarity).`
`BINDING`	`91 91`		`NADP (By similarity).`
`BINDING`	`136 136`		`NADP; via carbonyl oxygen (By similarity).`
`BINDING`	`239 239`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`254 254`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`290 290`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`372 372`		`NADP (By similarity).`
`SITE`	`236 236`	`1`	`Activates thiol group during catalysis (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 392 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 41863 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 35647D90B542D047 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NSSLQVSNKG FSEFSGLRTS SAIPFGRKTN DDLLSVVAFQ TSVIGGGNSK RGVVEAKLKV 

        70         80         90        100        110        120 
AINGFGRIGR NFLRCWHGRK DSPLDVIAIN DTGGVKQASH LLKYDSTLGI FDADVKPVGT 

       130        140        150        160        170        180 
DGISVDGKVI QVVSDRNPVN LPWGDLGIDL VIEGTGVFVD REGAGKHIQA GAKKVLITAP 

       190        200        210        220        230        240 
GKGDIPTYVV GVNADLYNPD EPIISNASCT TNCLAPFVKV LDQKFGIIKG TMTTTHSYTG 

       250        260        270        280        290        300 
DQRLLDASHR DLRRARAAAL NIVPTSTGAA KAVALSSQAL RGSSMALPLR VPTPNVSVVD 

       310        320        330        340        350        360 
LVVQVSKKTF AEEVNAAFRE AADKELKGIL DVCDEPLVSV DFRCSDVSST VDASLTMVMG 

       370        380        390 
DDMVKVIAWY DNEWGYSQRV VDLADIVANQ WK

P09043 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