NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3530755 [NCBI, ExPASy, EBI, Israel, Japan]
Martin W.F., Cerff R.;
"Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from mustard (Sinapis alba).";
Eur. J. Biochem. 159:323-331(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

X04302; CAA27845.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B24796; B24796.

3D structure databases

HSSP

P19866; 1NBO. [HSSP ENTRY / PDB]

SMR

P09672; 1-233.

ModBase

P09672.

Family and domain databases

InterPro

IPR000173; GlycerAld_3-P_DHase.
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.

PS00071; GAPDH; 1.

Other

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

Keywords

Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 233`	`>233`	`Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic.`	`PRO_0000145617`
`REGION`	`49 51`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`108 109`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`80 80`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`95 95`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`131 131`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`213 213`		`NADP (By similarity).`
`SITE`	`77 77`	`1`	`Activates thiol group during catalysis (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 233 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 25103 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: EE1502C53AC556F3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DREGAGKHIQ AGAKKVLITA PGKGDIPTYV VGVNAELYSH EDTIISNASC TTNCLAPFVK 

        70         80         90        100        110        120 
VLDQKFGIIK GTMTTTHSYT GDQRLLDASH RDLRRARAAA LNIVPTSTGA AKAVALVLPN 

       130        140        150        160        170        180 
LKGKLNGIAL RVPTPNVSVV DLVVQVSKKT FAEEVNAAFR DAAEKELKGI LDVCDEPLVS 

       190        200        210        220        230 
VDFRCSDVSS TIDSSLTMVM GDDMVKVIAW YDNEWGYSQR VVDLADIVAN NWK

P09672 in FASTA format

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View entry in raw text format (no links)
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	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