NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(92)90126-A; PubMed=1446820 [NCBI, ExPASy, EBI, Israel, Japan]
Lee Y.H., Huang X.Y., Hirsh D., Fox G.E., Hecht R.M.;
"Conservation of gene organization and trans-splicing in the glyceraldehyde-3-phosphate dehydrogenase-encoding genes of Caenorhabditis briggsae.";
Gene 121:227-235(1992).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AF16;
DOI=10.1371/journal.pbio.0000045; PubMed=14624247 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics.";
PLoS Biol. 1:166-192(2003).

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: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
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

M86669; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
CAAC02000521; CAP32766.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0769; JH0769.

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

SMR

P32809; 3-340.

ModBase

P32809.

Organism-specific databases

WormBase

WBGene00000332; Cbr-gpd-3.2.

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.

PIRSF

PIRSF000149; GAP_DH; 1.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PROSITE

PS00071; GAPDH; 1.

BLOCKS

P32809.

Genome annotation databases

Ensembl

ENSCBRG00000002093; Caenorhabditis briggsae. [Contig view]

Other

ProtoNet

P32809.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 341`	`341`	`Glyceraldehyde-3-phosphate dehydrogenase 2.`	`PRO_0000145508`
`NP_BIND`	`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).`
`ACT_SITE`	`158 158`		`Nucleophile (By similarity).`
`BINDING`	`35 35`		`NAD (By similarity).`
`BINDING`	`85 85`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`188 188`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`240 240`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`322 322`		`NAD (By similarity).`
`SITE`	`185 185`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 36509 Da [This is the MW of the unprocessed precursor]

CRC64: C93984A33A4A253E [This is a checksum on the sequence]

        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

P32809 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