NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Horst U3;
DOI=10.1007/BF00326409; PubMed=1473176 [NCBI, ExPASy, EBI, Israel, Japan]
Harmsen M.C., Schuren F.H.J., Moukha S.M., van Zuilen C.M., Punt P.J., Wessels J.G.H.;
"Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus.";
Curr. Genet. 22:447-454(1992).

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

M81728; AAA32634.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26976; S26976.

3D structure databases

HSSP

P00357; 4GPD. [HSSP ENTRY / PDB]

ModBase

P32636.

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`	`1 338`	`338`	`Glyceraldehyde-3-phosphate dehydrogenase 2.`	`PRO_0000145534`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`149 151`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`209 210`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`150 150`		`Nucleophile (By similarity).`
`BINDING`	`33 33`		`NAD (By similarity).`
`BINDING`	`78 78`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`180 180`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`232 232`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`314 314`		`NAD (By similarity).`
`SITE`	`177 177`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 36570 Da [This is the MW of the unprocessed precursor]

CRC64: 3381DBBF73B84469 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKVGINGFG RIGRIVLRNA LQFQDIEVVA VNDPFIDLEY MAYMFKYDSV HGRFKGTVEV 

        70         80         90        100        110        120 
KNGSFVVDGR PMKVFAERDP AAIPWGSVGA DYVVESTGVF TTIDKASAHL KGGAKKVVIS 

       130        140        150        160        170        180 
APSADAPMYV CGVNLDKYNP KDTIISNASC TTNCLATLAK VIHDNFGIVE GLMTTVHATT 

       190        200        210        220        230        240 
ATQKTVDGPS HKDWRGGRGV GNNIIPSSTG AAKAVGKVIP SLNGKLTGLS MRVPTQDVSV 

       250        260        270        280        290        300 
VDLVVRLEKP ASYEQIKEVM RKAAEGEYKG IIAYTDEDVV STDFISDNNS CVFDAKAGIQ 

       310        320        330 
LSPNFVKLIA WYDNEWGYSR RVCNLLQYVA KEDAKAGI

P32636 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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