[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Seedling; DOI=10.1007/BF00027337; PubMed=2562762 [NCBI, ExPASy, EBI, Israel, Japan] Brinkmann H., Cerff R., Salomon M., Soll J.; "Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach."; Plant Mol. Biol. 13:81-94(1989).
[2]	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).
[3]	PROTEIN SEQUENCE OF 83-451. 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).

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

X15189; CAA33263.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76553; AAD10218.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S05553; DESPGB.

3D structure databases

PDB

2PKQ; X-ray; 3.60 A; O/Q/T=84-451.

[ExPASy / RCSB / EBI]

PDBsum

2PKQ; -.

ModBase

P12860.

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

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 83`	`83`	`Chloroplast.`
`CHAIN`	`84 451`	`368`	`Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic.`	`PRO_0000010426`
`NP_BIND`	`94 95`	`2`	`NADP (By similarity).`
`REGION`	`237 239`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`296 297`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`238 238`		`Nucleophile (By similarity).`
`BINDING`	`118 118`		`NADP (By similarity).`
`BINDING`	`163 163`		`NADP; via carbonyl oxygen (By similarity).`
`BINDING`	`268 268`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`283 283`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`319 319`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`402 402`		`NADP (By similarity).`
`SITE`	`265 265`	`1`	`Activates thiol group during catalysis (By similarity).`
`STRAND`	`85 90`	`6`
`HELIX`	`95 104`	`10`
`STRAND`	`105 107`	`3`
`STRAND`	`110 117`	`8`
`HELIX`	`121 130`	`10`
`TURN`	`133 135`	`3`
`STRAND`	`142 145`	`4`
`TURN`	`146 148`	`3`
`STRAND`	`149 152`	`4`
`STRAND`	`155 160`	`6`
`HELIX`	`165 167`	`3`
`HELIX`	`170 173`	`4`
`STRAND`	`177 180`	`4`
`STRAND`	`182 184`	`3`
`HELIX`	`188 191`	`4`
`HELIX`	`193 197`	`5`
`STRAND`	`200 206`	`7`
`STRAND`	`209 213`	`5`
`STRAND`	`231 234`	`4`
`HELIX`	`240 251`	`12`
`TURN`	`252 254`	`3`
`STRAND`	`256 266`	`11`
`STRAND`	`273 275`	`3`
`TURN`	`281 284`	`4`
`HELIX`	`297 301`	`5`
`HELIX`	`302 305`	`4`
`HELIX`	`307 309`	`3`
`STRAND`	`318 321`	`4`
`STRAND`	`326 337`	`12`
`HELIX`	`341 352`	`12`
`TURN`	`353 356`	`4`
`HELIX`	`369 372`	`4`
`STRAND`	`380 382`	`3`
`HELIX`	`383 385`	`3`
`STRAND`	`390 400`	`11`
`HELIX`	`404 419`	`16`

Sequence information

Length: 451 AA [This is the length of the unprocessed precursor]

Molecular weight: 48126 Da [This is the MW of the unprocessed precursor]

CRC64: 45D826A6DA5B4837 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASHAALAPS RIPASTRLAS KASQQYSFLT QCSFKRLDVA DFSGLRSSNS VTFTREASFH 

        70         80         90        100        110        120 
DVIAAQLTTK PTGAAPVRGE TVAKLKVAIN GFGRIGRNFL RCWHGRKDSP LDVVVVNDSG 

       130        140        150        160        170        180 
GVKSATHLLK YDSILGTFKA DVKIIDNETF SIDGKPIKVV SNRDPLKLPW AELGIDIVIE 

       190        200        210        220        230        240 
GTGVFVDGPG AGKHIQAGAK KVIITAPAKG SDIPTYVVGV NEKDYGHDVA NIISNASCTT 

       250        260        270        280        290        300 
NCLAPFVKVL DEELGIVKGT MTTTHSYTGD QRLLDASHRD LRRARAAALN IVPTSTGAAK 

       310        320        330        340        350        360 
AVSLVLPQLK GKLNGIALRV PTPNVSVVDL VVNIEKVGVT AEDVNNAFRK AAAGPLKGVL 

       370        380        390        400        410        420 
DVCDIPLVSV DFRCSDFSST IDSSLTMVMG GDMVKVVAWY DNEWGYSQRV VDLADLVANK 

       430        440        450 
WPGLEGSVAS GDPLEDFCKD NPADEECKLY E

P12860 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