NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, AND CHARACTERIZATION.
STRAIN=DSM 3773;
PubMed=2165475 [NCBI, ExPASy, EBI, Israel, Japan]
Zwickl P., Fabry S., Bogedain C., Haas A., Hensel R.;
"Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli.";
J. Bacteriol. 172:4329-4338(1990).

Comments

FUNCTION: Active in the presence of NAD and NADP.
CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)⁺ = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Thermostable. Has a 44 minutes half-life at 100 degrees Celsius;
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

M83988; AAA73180.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S10653; DEQYG.

3D structure databases

HSSP

P10618; 1CF2. [HSSP ENTRY / PDB]

SMR

P61880; 1-334.

ModBase

P61880.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0043891;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00559; -; 1.
PBIL [Tree]

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
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.

ProDom

PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01546; GAPDH-II_archae; 1.

PS00071; GAPDH; 1.

Other

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

Keywords

Cytoplasm; Direct protein sequencing; Glycolysis; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 334`	`334`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145733`
`NP_BIND`	`12 13`	`2`	`NAD (By similarity).`
`REGION`	`140 142`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`192 193`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`141 141`		`Nucleophile (By similarity).`
`BINDING`	`111 111`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`167 167`		`NAD (By similarity).`
`BINDING`	`298 298`		`NAD; via carbonyl oxygen (By similarity).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 37436 Da [This is the MW of the unprocessed precursor]

CRC64: 224E0626923AFC66 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIKVGINGY GTIGKRVAYA VTKQDDMELI GVTKTKPDFE AYRAKELGIP VYAASEEFLP 

        70         80         90        100        110        120 
RFEKAGFEVE GTLNDLLEKV DIIVDATPGG MGEKNKQLYE KAGVKAIFQG GEKAEVAQVS 

       130        140        150        160        170        180 
FVAQANYEAA LGKDYVRVVS CNTTGLVRTL NAIKDYVDYV YAVMIRRAAD PNDIKRGPIN 

       190        200        210        220        230        240 
AIKPSVTIPS HHGPDVQTVI PINIETSAFV VPTTIMHVHS IMVELKKPLT REDVIDIFEN 

       250        260        270        280        290        300 
TTRVLLFEKE KGFESTAQLI EFARDLHREW NNLYEIAVWK ESINVKGNRL FYIQAVHQES 

       310        320        330 
DVIPENIDAI RAMFEIAEKW ESIKKTNKSL GILK

P61880 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