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

M81727; AAA32633.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26975; S26975.

3D structure databases

HSSP

P56649; 1CRW. [HSSP ENTRY / PDB]

ModBase

P32635.

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`	`1 337`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000145533`
`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`	`318 318`		`NAD (By similarity).`
`SITE`	`177 177`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 36749 Da [This is the MW of the unprocessed precursor]

CRC64: FBA09EE1A75A4D3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVNVGINGFG RIGRLVLRNA LQMQILTVVA VNDPFLDVEY MAYLFKYDSV HGRYQGKVET 

        70         80         90        100        110        120 
KDGKLIIDGH KIAAFAEREP ANIKWADCGA EYIVESTGVF KTEELAKEHL KGGAKKVVIT 

       130        140        150        160        170        180 
APGSGVPTYV VGVNLDKYDP KEVVISNASC TTNCLAVLAK VINDKFGIVE GLMTTVHATT 

       190        200        210        220        230        240 
ATQKTVDAPA KKDWRSGRSV TNNIIPASTG AAKAVTKAIP DLEGKLTGLA FRVPTLDVSV 

       250        260        270        280        290        300 
VDLVVRLEKE TSYDDVKKAM RDAADGKHPG IEKGIVDYTE EDVVSTDFVG SNYSMIFDAK 

       310        320        330 
AGIALNSRFM KLVAWYDNEW GYARRVCDEV VYVAKKN

P32635 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