[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1023/A:1017035109224; PubMed=9720289 [NCBI, ExPASy, EBI, Israel, Japan] Zeng L.-W., Comeron J.M., Chen B., Kreitman M.; "The molecular clock revisited: the rate of synonymous vs. replacement change in Drosophila."; Genetica 102:369-382(1998).

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

AF025810; AAB87895.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

SMR

O44105; 1-304.

ModBase

O44105.

Organism-specific databases

FlyBase

FBgn0012937; Dsub\Gapdh2.

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 >304`	`>304`	`Glyceraldehyde-3-phosphate dehydrogenase 2.`	`PRO_0000145525`
`NP_BIND`	`1 2`	`2`	`NAD (By similarity).`
`REGION`	`138 140`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`198 199`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`139 139`		`Nucleophile (By similarity).`
`BINDING`	`22 22`		`NAD (By similarity).`
`BINDING`	`67 67`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`169 169`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`221 221`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`303 303`		`NAD (By similarity).`
`SITE`	`166 166`	`1`	`Activates thiol group during catalysis (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`304 304`

Sequence information

Length: 304 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 32176 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 9BE9C70576089D1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVVAE GGFLVVNGQK 

        70         80         90        100        110        120 
ITVFSERDPA NINWASAGAE YVVESTGVFT TIEKASTHLK GGAKKVVISA PSADAPMFVC 

       130        140        150        160        170        180 
GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG 

       190        200        210        220        230        240 
KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA 

       250        260        270        280        290        300 
SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL NDKFVKLISW 


YDNE

O44105 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