NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(88)90334-4; PubMed=2841192 [NCBI, ExPASy, EBI, Israel, Japan]
Fabry S., Hensel R.;
"Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus.";
Gene 64:189-197(1988).

[2]

X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
DOI=10.1006/jmbi.2000.3565; PubMed=10715215 [NCBI, ExPASy, EBI, Israel, Japan]
Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G., Vitoux B., Aubry A.;
"The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution.";
J. Mol. Biol. 297:481-500(2000).

Comments

FUNCTION: Exhibits a dual-cofactor specificity, with a marked preference for NADP(+) over NAD(+).
CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)⁺ = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
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

M19980; AAA88227.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JT0286; JT0286.

3D structure databases

PDB

1CF2; X-ray; 2.10 A; O/P/Q/R=1-337.

[ExPASy / RCSB / EBI]

PDBsum

1CF2; -.

ModBase

P10618.

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:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00559; atypical; 1.
PBIL [Tree]

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
Graphical view of domain structure.

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.

PROSITE

PS00071; GAPDH; 1.

Other

ProtoNet

P10618.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 337`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145722`
`NP_BIND`	`11 12`	`2`	`NADP.`
`NP_BIND`	`34 35`	`2`	`NADP.`
`REGION`	`139 141`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`194 195`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`140 140`		`Nucleophile (By similarity).`
`BINDING`	`110 110`		`NADP; via amide nitrogen.`
`BINDING`	`171 171`		`NADP.`
`BINDING`	`300 300`		`NADP; via carbonyl oxygen (By similarity).`
`STRAND`	`2 7`	`6`
`HELIX`	`11 21`	`11`
`STRAND`	`23 35`	`13`
`HELIX`	`38 45`	`8`
`STRAND`	`50 54`	`5`
`HELIX`	`55 57`	`3`
`HELIX`	`58 63`	`6`
`HELIX`	`72 77`	`6`
`STRAND`	`80 84`	`5`
`HELIX`	`90 100`	`11`
`STRAND`	`104 107`	`4`
`HELIX`	`113 116`	`4`
`HELIX`	`122 129`	`8`
`STRAND`	`133 137`	`5`
`HELIX`	`140 156`	`17`
`STRAND`	`158 170`	`13`
`STRAND`	`184 191`	`8`
`HELIX`	`194 199`	`6`
`STRAND`	`206 214`	`9`
`STRAND`	`219 229`	`11`
`HELIX`	`233 242`	`10`
`STRAND`	`246 249`	`4`
`TURN`	`251 254`	`4`
`HELIX`	`258 268`	`11`
`HELIX`	`271 273`	`3`
`STRAND`	`277 281`	`5`
`HELIX`	`282 284`	`3`
`STRAND`	`286 288`	`3`
`STRAND`	`291 298`	`8`
`TURN`	`300 304`	`5`
`HELIX`	`305 315`	`11`
`HELIX`	`322 333`	`12`

Sequence information

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

Molecular weight: 37408 Da [This is the MW of the unprocessed precursor]

CRC64: D83CBA88AAE5B0B8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL YVAIPERVKL 

        70         80         90        100        110        120 
FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE KGIKAIFQGG EKHEDIGLSF 

       130        140        150        160        170        180 
NSLSNYEESY GKDYTRVVSC NTTGLCRTLK PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI 

       190        200        210        220        230        240 
NAIIPNPPKL PSHHGPDVKT VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF 

       250        260        270        280        290        300 
EDTPRVILIS AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ 

       310        320        330 
ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ

P10618 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