[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00019102; PubMed=8980499 [NCBI, ExPASy, EBI, Israel, Japan] Baalmann E., Scheibe R., Cerff R., Martin W.; "Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase subunits A and B expressed in Escherichia coli: formation of highly active A4 and B4 homotetramers and evidence that aggregation of the B4 complex is mediated by the B subunit carboxy terminus."; Plant Mol. Biol. 32:505-513(1996).
[2]	PROTEIN SEQUENCE OF 66-401. DOI=10.1016/0167-4838(90)90119-Z; PubMed=2223845 [NCBI, ExPASy, EBI, Israel, Japan] Ferri G., Stoppini M., Meloni M.L., Zapponi M.C., Iadarola P.; "Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II."; Biochim. Biophys. Acta 1041:36-42(1990).
[3]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 66-401 IN COMPLEX WITH NAD, AND SUBUNIT. DOI=10.1021/bi0272149; PubMed=12705826 [NCBI, ExPASy, EBI, Israel, Japan] Falini G., Fermani S., Ripamonti A., Sabatino P., Sparla F., Pupillo P., Trost P.; "Dual coenzyme specificity of photosynthetic glyceraldehyde-3-phosphate dehydrogenase interpreted by the crystal structure of A4 isoform complexed with NAD."; Biochemistry 42:4631-4639(2003).
[4]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 66-401 IN COMPLEX WITH NADP, MUTAGENESIS OF THR-101 AND SER-257, AND SUBUNIT. DOI=10.1016/j.jmb.2004.06.005; PubMed=15236965 [NCBI, ExPASy, EBI, Israel, Japan] Sparla F., Fermani S., Falini G., Zaffagnini M., Ripamonti A., Sabatino P., Pupillo P., Trost P.; "Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited by oxidized thioredoxin."; J. Mol. Biol. 340:1025-1037(2004).

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).
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

L76552; AAD10217.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09012; T09012.

3D structure databases

PDB

1JN0; X-ray; 3.00 A; A/B/O=66-401.	[ExPASy / RCSB / EBI]
1NBO; X-ray; 2.60 A; A/B/O=66-401.	[ExPASy / RCSB / EBI]
1RM3; X-ray; 2.20 A; A/B/O=66-401.	[ExPASy / RCSB / EBI]
1RM4; X-ray; 2.00 A; A/B/O=66-401.	[ExPASy / RCSB / EBI]
1RM5; X-ray; 2.10 A; A/B/O=66-401.	[ExPASy / RCSB / EBI]
2HKI; X-ray; 3.00 A; A=66-401.	[ExPASy / RCSB / EBI]
2PKQ; X-ray; 3.60 A; P/R/S=66-401.	[ExPASy / RCSB / EBI]
2PKR; X-ray; 2.40 A; A/B/C/D/H/I/L/M/O/P/Q/R=66-401.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JN0; -.
1NBO; -.
1RM3; -.
1RM4; -.
1RM5; -.
2HKI; -.
2PKQ; -.
2PKR; -.

ModBase

P19866.

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

3D-structure; Calvin cycle; Chloroplast; Direct protein sequencing; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 65`	`65`	`Chloroplast.`
`CHAIN`	`66 401`	`336`	`Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic.`	`PRO_0000010425`
`NP_BIND`	`76 77`	`2`	`NADP.`
`REGION`	`217 219`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`276 277`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`218 218`		`Nucleophile.`
`BINDING`	`100 100`		`NADP.`
`BINDING`	`145 145`		`NADP; via carbonyl oxygen.`
`BINDING`	`248 248`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`263 263`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`299 299`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`381 381`		`NADP.`
`SITE`	`245 245`	`1`	`Activates thiol group during catalysis (By similarity).`
`MUTAGEN`	`101 101`		`T->A: Reduced affinity for NADP, and slight increase of the affinity for NAD.`
`MUTAGEN`	`257 257`		`S->A: Reduced affinity for NADP, and slight increase of the affinity for NAD.`
`CONFLICT`	`288 288`		`N -> Q (in Ref. 2; AA sequence).`
`CONFLICT`	`401 401`		`Q -> QA (in Ref. 2; AA sequence).`
`STRAND`	`68 72`	`5`
`HELIX`	`76 87`	`12`
`STRAND`	`88 90`	`3`
`STRAND`	`94 99`	`6`
`HELIX`	`104 112`	`9`
`TURN`	`115 117`	`3`
`STRAND`	`124 126`	`3`
`STRAND`	`130 134`	`5`
`STRAND`	`137 142`	`6`
`HELIX`	`147 149`	`3`
`HELIX`	`152 155`	`4`
`STRAND`	`158 162`	`5`
`STRAND`	`164 166`	`3`
`HELIX`	`170 178`	`9`
`STRAND`	`182 188`	`7`
`TURN`	`199 201`	`3`
`HELIX`	`203 205`	`3`
`STRAND`	`211 214`	`4`
`HELIX`	`218 234`	`17`
`STRAND`	`236 246`	`11`
`STRAND`	`253 255`	`3`
`TURN`	`261 264`	`4`
`TURN`	`267 269`	`3`
`STRAND`	`272 275`	`4`
`HELIX`	`278 285`	`8`
`HELIX`	`287 289`	`3`
`TURN`	`290 292`	`3`
`STRAND`	`293 301`	`9`
`STRAND`	`306 316`	`11`
`HELIX`	`320 332`	`13`
`TURN`	`333 338`	`6`
`STRAND`	`339 342`	`4`
`HELIX`	`348 351`	`4`
`STRAND`	`356 361`	`6`
`HELIX`	`362 364`	`3`
`STRAND`	`366 368`	`3`
`TURN`	`369 371`	`3`
`STRAND`	`372 379`	`8`
`HELIX`	`383 398`	`16`

Sequence information

Length: 401 AA [This is the length of the unprocessed precursor]

Molecular weight: 43023 Da [This is the MW of the unprocessed precursor]

CRC64: 2A815842EA095A84 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASNMLSIAN PSLRVYNKGF SEFSGLHTSS LPFGRKGSDD LMAFVSFQTN AVGGKRSSQN 

        70         80         90        100        110        120 
GVVEAKLKVA INGFGRIGRN FLRCWHGRKD SPLDVVVIND TGGVKQASHL LKYDSILGTF 

       130        140        150        160        170        180 
DADVKTAGDS AISVDGKVIK VVSDRNPVNL PWGDMGIDLV IEGTGVFVDR DGAGKHLQAG 

       190        200        210        220        230        240 
AKKVLITAPG KGDIPTYVVG VNEEGYTHAD TIISNASCTT NCLAPFVKVL DQKFGIIKGT 

       250        260        270        280        290        300 
MTTTHSYTGD QRLLDASHRD LRRARAACLN IVPTSTGAAK AVALVLPNLK GKLNGIALRV 

       310        320        330        340        350        360 
PTPNVSVVDL VVQVSKKTFA EEVNAAFRES ADNELKGILS VCDEPLVSID FRCTDVSSTI 

       370        380        390        400 
DSSLTMVMGD DMVKVIAWYD NEWGYSQRVV DLADIVANKW Q

P19866 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