NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Ro1 / Mierenbos;
DOI=10.1016/S0166-6851(98)00108-X; PubMed=9851607 [NCBI, ExPASy, EBI, Israel, Japan]
Qin L., Smant G., Stokkermans J.P.W.G., Bakker J., Schots A., Helder J.;
"Cloning of a trans-spliced glyceraldehyde-3-phosphate-dehydrogenase gene from the potato cyst nematode Globodera rostochiensis and expression of its putative promoter region in Caenorhabditis elegans.";
Mol. Biochem. Parasitol. 96:59-67(1998).

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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AF004522; AAC79129.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00354; 3GPD. [HSSP ENTRY / PDB]

SMR

O16027; 3-324.

ModBase

O16027.

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.

PS00071; GAPDH; 1.

Other

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

Keywords

Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >324`	`>324`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000145516`
`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).`
`NON_TER`	`324 324`

Sequence information

Length: 324 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 34580 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 1815C606CBBE1039 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKPKVGING FGRIGRLALR AAVEKDTVQV VAINDPFIEL DYMVYMFNYD STHGRFNGKI 

        70         80         90        100        110        120 
STSAGNLVVE KEGKATHTIK VFNLKDPAEI KWAEVGAEYV IESTGVFTTI EKASAHLKGG 

       130        140        150        160        170        180 
AKKVVISAPS ADAPMYVMGV NEDKYDPAKD NVISNASCTT NCLAPLAKVI NDEFGIIEGL 

       190        200        210        220        230        240 
MTTVHAVTAT QKTVDGPNGK QWRDGRGAAQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR 

       250        260        270        280        290        300 
VPTPNVSVVD LTARLEKPAS LDAIKAAVKK AAEGNLKGIL GYTEDQVVST DFLGDSRSSI 

       310        320 
FDAGACISLN PHFVKLVSWY DNEF

O16027 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