NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2492940 [NCBI, ExPASy, EBI, Israel, Japan]
Fabry S., Lang J., Niermann T., Vingron M., Hensel R.;
"Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Comparison with the respective gene structure of the closely related extreme thermophile Methanothermus fervidus.";
Eur. J. Biochem. 179:405-413(1989).

Comments

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 (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

X14632; CAB37402.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S02803; S02803.

3D structure databases

HSSP

P10618; 1CF2. [HSSP ENTRY / PDB]

SMR

P19315; 1-338.

ModBase

P19315.

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: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; -; 1.
PBIL [Tree]

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

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.

PS00071; GAPDH; 1.

Other

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

Keywords

Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 338`	`338`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145721`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`140 142`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`195 196`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`141 141`		`Nucleophile (By similarity).`
`BINDING`	`111 111`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`169 169`		`NAD (By similarity).`
`BINDING`	`302 302`		`NAD; via carbonyl oxygen (By similarity).`

Sequence information

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

Molecular weight: 37220 Da [This is the MW of the unprocessed precursor]

CRC64: 8F96B2DC638A1CFE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKSVGINGYG TIGKRVADAV SAQDDMKIVG VTKRSPDFEA RMAVEKGYDL YISAPERENS 

        70         80         90        100        110        120 
FEEAGIKVTG TAEELFEKLD IVVDCTPEGI GAKNKEGTYE KMGLKATFQG GEKHDQIGLS 

       130        140        150        160        170        180 
FNSFSNYKDV IGKDYARVVS CNTTGLCRTL NPINDLCGIK KVRAVMVRRG ADPSQVKKGP 

       190        200        210        220        230        240 
INAIVPNPPT VPSHHGPDVQ TVMYDLNITT MALLVPTTLM HQHNLMVELE SSVSIDDIKD 

       250        260        270        280        290        300 
KLNETPRVLL LKAKEGLGST AEFMEYAKEL GRSRNDLFEI GVWEESLNIV DGELYYMQAI 

       310        320        330 
HQESDVVPEN VDAIRAMLEM EDNPSKSIEK TNKAMGIL

P19315 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