P32809 (G3P2_CAEBR) 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
Synonyms:	gpd-3.2
ORF Names:	CBG14137

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [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.
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	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 – 341	341	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145508
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

Sequences

	Sequence		Length	Mass (Da)
	P32809 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: C93984A33A4A253E	FASTA	341	36,509
	10 20 30 40 50 60 MSKPTVGING FGRIGRLVLR AAVEKDSVNV VAVNDPFISI DYMVYLFQYD STHGRFKGTV 70 80 90 100 110 120 KHEGDYLIVA NEGKSQHKIK VYNSKDPAEI QWGAAGADYV 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 LDDIKRVIKA AAEGPLKGVL AYTEDQVVST DFVSDTHSSI 310 320 330 340 FDAGASIILN PNFVKLISWY DNEFGYSNRV VDLISYIATK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of gene organization and trans-splicing in the glyceraldehyde-3-phosphate dehydrogenase-encoding genes of Caenorhabditis briggsae." Lee Y.H., Huang X.Y., Hirsh D., Fox G.E., Hecht R.M. Gene 121:227-235(1992) [PubMed: 1446820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M86669 Genomic DNA. No translation available. CAAC02000521 Genomic DNA. Translation: CAP32766.1.
PIR	JH0769.
RefSeq	XP_002644328.1. XM_002644282.1.
3D structure databases
ProteinModelPortal	P32809.
SMR	P32809. Positions 3-340.
ModBase	Search...
Protein-protein interaction databases
STRING	P32809.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8586323.
KEGG	cbr:CBG14137.
Organism-specific databases
CTD	8586323.
WormBase	CBG14137; CBP18173; WBGene00000332.
Phylogenomic databases
HOGENOM	HBG571736.
OMA	YLIVANE.
PhylomeDB	P32809.
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...

Entry information

Entry name

G3P2_CAEBR

Accession

Primary (citable) accession number: P32809
Secondary accession number(s): A8XJE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project