NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665;
PubMed=7668042 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P.;
"Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene family from Kluyveromyces marxianus -- polymerase chain reaction-single-strand conformation polymorphism as a tool for the study of multigenic families.";
Yeast 11:725-733(1995).

[2]

X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665;
DOI=10.1074/jbc.M605267200; PubMed=16963457 [NCBI, ExPASy, EBI, Israel, Japan]
Ferreira-da-Silva F., Pereira P.J.B., Gales L., Roessle M., Svergun D.I., Moradas-Ferreira P., Damas A.M.;
"The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures.";
J. Biol. Chem. 281:33433-33440(2006).

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

PIR

S57279; S57279.

3D structure databases

PDB

2I5P; X-ray; 2.30 A; O/P=1-329.

[ExPASy / RCSB / EBI]

2I5P; -.

P84998; 1-329.

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

3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 329`	`329`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000253990`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`148 150`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`208 209`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`149 149`		`Nucleophile (By similarity).`
`BINDING`	`33 33`		`NAD (By similarity).`
`BINDING`	`77 77`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`179 179`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`231 231`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`313 313`		`NAD (By similarity).`
`SITE`	`176 176`	`1`	`Activates thiol group during catalysis (By similarity).`
`MOD_RES`	`148 148`		`Phosphoserine (By similarity).`
`MOD_RES`	`177 177`		`Phosphoserine (By similarity).`
`MOD_RES`	`200 200`		`Phosphoserine (By similarity).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35253 Da [This is the MW of the unprocessed precursor]

CRC64: 4C5C08D5C7858672 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSIAINGFG RIGRLVLRIA LERKNIDVVA INDPFISVDY AAYMFKYDST HGKYKGEVSH 

        70         80         90        100        110        120 
DGSNLIINGK KVAVFQEKDP ATLPWGKLGV DIAVDSTGVF KELDSAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSKTAPMFV VGVNEDKYNG EKIVSNASCT TNCLAPIAKI INDEFGIEEG LMTTVHSITA 

       190        200        210        220        230        240 
TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTTDVSVV 

       250        260        270        280        290        300 
DLTVKLVKAA TYDEIKAAVK KVSEGKLKDV VGYTEDAVVS SDFLGDTHST IFDAAAGIQL 

       310        320 
SPKFVKLVAW YDNEYGYSTR VVDLVEHVA

P84998 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