P34922 (G3PC_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
EC=1.2.1.12

Gene names

Name:

GAPC1

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
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.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Glyceraldehyde-3-phosphate dehydrogenase, cytosolic		PRO_0000145610
Regions
	Nucleotide binding	14 – 15	2	NAD By similarity
	Region	154 – 156	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	214 – 215	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	155	1	Nucleophile By similarity
	Binding site	36	1	NAD By similarity
	Binding site	83	1	NAD; via carbonyl oxygen By similarity
	Binding site	185	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	237	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	319	1	NAD By similarity
	Site	182	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34922 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 09B55960BE03EA27	FASTA	338	36,609
	10 20 30 40 50 60 MGAKIKIGIN GFGRIGRLVA RVALKRDDVE LVAVNDPFIT TDYMTYMFKY DSVHGQWKND 70 80 90 100 110 120 ELTVKDSNTL LFGQKPVTVF AHRNPEEIPW ASTGADIIVE STGVFTDKDK AAAHLKGGAK 130 140 150 160 170 180 KVIISAPSKD APMFVVGVNE NEYKPEFDII SNASCTTNCL APLAKVINDR FGIVEGLMTT 190 200 210 220 230 240 VHSITATQKT VDGPSSKDWR GGRAASFNII PSSTGAAKAV GKVLPALNGK LTGMSFRVPT 250 260 270 280 290 300 VDVSVVDLTV RLEKAATYDE IKAAIKEESE GKLKGILGYT EDDVVSTDFI GDTRSSIFDA 310 320 330 KAGIALNDKF VKLVSWYDNE LGYSTRVVDL IVHIAKQL

References

[1]	"Molecular phylogenies in angiosperm evolution." Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R. Mol. Biol. Evol. 10:140-162(1993) [PubMed: 8095691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"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: cv. Rosakrone.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07500 mRNA. Translation: AAA33667.1. X73150 Genomic DNA. Translation: CAA51675.1.
PIR	T06781.
3D structure databases
ProteinModelPortal	P34922.
SMR	P34922. Positions 4-337.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR020831. GlycerAld/Erythrose_P_DH. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3PC_PEA

Accession

Primary (citable) accession number: P34922

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	December 14, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program