Reviewed, UniProtKB/Swiss-Prot P50362 (G3PA_CHLRE)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic
    EC=1.2.1.13
Alternative name(s):
    NADP-dependent glyceraldehydephosphate dehydrogenase subunit A

Gene names

Name:

GAPA

Organism

Chlamydomonas reinhardtii

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH.
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homotetramer. Component of a complex that contains two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH, causing its conformation to change. This GAPDH/CP12 complex binds PRK to form a half-complex (one unit). This unit probably dimerizes due partially to interactions between the enzymes of each unit.
Subcellular location	Plastid › chloroplast.
Miscellaneous	GAPDHB, the second subunit found in plants, is absent in algae. Algae contain three forms of GAPDH: two cytosolic forms which participate in glycolysis and one chloroplastic form which participates in photosynthesis. These three forms are encoded by distinct genes.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Calvin cycle
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Inferred from electronic annotation. Source: EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 34

34

Chloroplast By similarity

Chain

35 – 374

340

Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic

PRO_0000010418

Regions

Nucleotide binding

47 – 48

2

NADP By similarity

Region

189 – 191

3

Glyceraldehyde 3-phosphate binding By similarity

Region

248 – 249

2

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

190

1

Nucleophile By similarity

Binding site

71

1

NADP By similarity

Binding site

116

1

NADP; via carbonyl oxygen By similarity

Binding site

220

1

Glyceraldehyde 3-phosphate By similarity

Binding site

235

1

Glyceraldehyde 3-phosphate By similarity

Binding site

271

1

Glyceraldehyde 3-phosphate By similarity

Binding site

353

1

NADP By similarity

Site

217

1

Activates thiol group during catalysis By similarity

Amino acid modifications

Disulfide bond

55 ↔ 325

By similarity

Secondary structure

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374

Helix Strand Turn

Details...

Beta strand

37 – 43

7

Turn

45 – 47

3

Helix

48 – 54

7

Turn

55 – 59

5

Beta strand

64 – 73

10

Helix

75 – 83

9

Turn

86 – 88

3

Beta strand

100 – 104

5

Turn

124 – 127

4

Beta strand

129 – 133

5

Beta strand

135 – 137

3

Helix

141 – 144

4

Helix

146 – 151

6

Beta strand

153 – 160

8

Turn

171 – 173

3

Beta strand

174 – 177

4

Beta strand

184 – 186

3

Helix

190 – 205

16

Beta strand

208 – 217

10

Beta strand

220 – 223

4

Beta strand

225 – 227

3

Helix

233 – 236

4

Turn

239 – 241

3

Beta strand

244 – 246

3

Helix

250 – 257

8

Beta strand

262 – 271

10

Beta strand

278 – 290

13

Helix

294 – 302

9

Turn

303 – 310

8

Beta strand

311 – 316

6

Helix

321 – 323

3

Beta strand

327 – 333

7

Turn

334 – 336

3

Beta strand

341 – 351

11

Helix

355 – 371

17

Sequences

	Sequence		Length	Mass (Da)
	P50362-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8CEB02897930D34C	FASTA	374	40,304
	10 20 30 40 50 60 MAAMMQKSAF TGSAVSSKSG VRAKAARAVV DVRAEKKIRV AINGFGRIGR NFLRCWHGRQ 70 80 90 100 110 120 NTLLDVVAIN DSGGVKQASH LLKYDSTLGT FAADVKIVDD SHISVDGKQI KIVSSRDPLQ 130 140 150 160 170 180 LPWKEMNIDL VIEGTGVFID KVGAGKHIQA GASKVLITAP AKDKDIPTFV VGVNEGDYKH 190 200 210 220 230 240 EYPIISNASC TTNCLAPFVK VLEQKFGIVK GTMTTTHSYT GDQRLLDASH RDLRRARAAA 250 260 270 280 290 300 LNIVPTTTGA AKAVSLVLPS LKGKLNGIAL RVPTPTVSVV DLVVQVEKKT FAEEVNAAFR 310 320 330 340 350 360 EAANGPMKGV LHVEDAPLVS IDFKCTDQST SIDASLTMVM GDDMVKVVAW YDNEWGYSQR 370 VVDLAEVTAK KWVA

References

[1]	"Five identical intron positions in ancient duplicated genes of eubacterial origin." Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R. Nature 367:387-389(1994) [PubMed: 8114942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1132.
[2]	"The small protein CP12: a protein linker for supramolecular complex assembly." Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B. Biochemistry 42:8163-8170(2003) [PubMed: 12846565] [Abstract] Cited for: SUBUNIT, INTERACTION WITH CP12.
[3]	"Characterization of native and recombinant A4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for conformation changes upon association with the small protein CP12." Graciet E., Lebreton S., Camadro J.-M., Gontero B. Eur. J. Biochem. 270:129-136(2003) [PubMed: 12492483] [Abstract] Cited for: INTERACTION WITH CP12.
[4]	"Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate dehydrogenase contains the cysteine residues identified as potentially domain-locking in the higher plant enzyme and is light activated." Li A.D., Stevens F.J., Huppe H.C., Kersanach R., Anderson L.E. Photosyn. Res. 51:167-177(1997) Cited for: 3D-STRUCTURE MODELING OF 35-374.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L27668 Genomic DNA. Translation: AAA86855.1.

PIR

T07990.

RefSeq

XP_001689871.1.

UniGene

Cre.2829

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NLG	model	-	A	35-374	[»]
1NLH	model	-	A	35-374	[»]

SMR

P50362. Positions 37-372.

ModBase

Search...

Genome annotation databases

GeneID

5715019.

KEGG

cre:CHLREDRAFT_129019.

Family and domain databases

InterPro

IPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_1.
[Graphical view]

PANTHER

PTHR10836. GAP_DH. 1 hit.

Pfam

PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000149. GAP_DH. 1 hit.

PRINTS

PR00078. G3PDHDRGNASE.

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G3PA_CHLRE

Accession

Primary (citable) accession number: P50362

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)