P17329 (G3P2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 2
Short name=GAPDH-2
EC=1.2.1.12

Gene names

Name:	gpd-2
ORF Names:	K10B3.8

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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	There are four nearly identical glyceraldehyde 3-phosphate dehydrogenases in Caenorhabditis elegans.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	determination of adult lifespan Inferred from mutant phenotype. Source: WormBase glycolysis Inferred from electronic annotation. Source: UniProtKB-KW lipid storage Inferred from mutant phenotype. Source: WormBase
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 – 341	341	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145511
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	157 – 159	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	217 – 218	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	158	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	85	1	NAD; via carbonyl oxygen By similarity
	Binding site	188	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	240	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	322	1	NAD By similarity
	Site	185	1	Activates thiol group during catalysis By similarity
Experimental info
	Sequence conflict	5	1	S → N in CAA33326. Ref.1
	Sequence conflict	31	1	V → D in CAA33326. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17329 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: E355331B65E39CF5	FASTA	341	36,455
	10 20 30 40 50 60 MPKPSVGING FGRIGRLVLR AAVEKDSVNV VAVNDPFISI DYMVYLFQYD STHGRFKGTV 70 80 90 100 110 120 AHEGDYLLVA KEGKSQHKIK VYNSRDPAEI QWGASGADYV VESTGVFTTI EKANAHLKGG 130 140 150 160 170 180 AKKVIISAPS ADAPMFVVGV NHEKYDHAND HIISNASCTT NCLAPLAKVI NDNFGIIEGL 190 200 210 220 230 240 MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR 250 260 270 280 290 300 VPTPDVSVVD LTARLEKPAS LDDIKKVIKA AADGPMKGIL AYTEDQVVST DFVSDTNSSI 310 320 330 340 FDAGASISLN PHFVKLVSWY DNEFGYSNRV VDLISYIATK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans." Huang X.Y., Barrios L.A.M., Vonkhorporn P., Honda S., Albertson D.G., Hecht R.M. J. Mol. Biol. 206:411-424(1989) [PubMed: 2716055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15254 Genomic DNA. Translation: CAA33326.1. FO080552 Genomic DNA. Translation: CCD64600.1.
PIR	A89491. DEKWG2. S03913.
RefSeq	NP_508535.1. NM_076134.4.
UniGene	Cel.23529.
3D structure databases
ProteinModelPortal	P17329.
SMR	P17329. Positions 6-340.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-26337N.
IntAct	P17329. 3 interactions.
MINT	MINT-229721.
STRING	P17329.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	K10B3.8.1; K10B3.8.1; K10B3.8. K10B3.8.2; K10B3.8.2; K10B3.8.
GeneID	3565504.
KEGG	cel:K10B3.8.
UCSC	K10B3.8.1. c. elegans.
Organism-specific databases
CTD	3565504.
WormBase	K10B3.8; CE07371; WBGene00001684; gpd-2.
Phylogenomic databases
eggNOG	meNOG07146.
GeneTree	EMGT00050000002948.
HOGENOM	HBG571736.
InParanoid	P17329.
OMA	KFYTERD.
PhylomeDB	P17329.
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.
KO	K00134.
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...
Other
NextBio	956731.

Entry information

Entry name

G3P2_CAEEL

Accession

Primary (citable) accession number: P17329

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	July 22, 2008
Last modified:	December 14, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project