[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8095691 [NCBI, ExPASy, EBI, Israel, Japan] Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R.; "Molecular phylogenies in angiosperm evolution."; Mol. Biol. Evol. 10:140-162(1993).

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

X72381; CAA51071.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

ModBase

P34923.

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`	`1 342`	`342`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145613`
`NP_BIND`	`16 17`	`2`	`NAD (By similarity).`
`REGION`	`155 157`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`215 216`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`156 156`		`Nucleophile (By similarity).`
`BINDING`	`38 38`		`NAD (By similarity).`
`BINDING`	`85 85`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`186 186`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`238 238`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`320 320`		`NAD (By similarity).`
`SITE`	`183 183`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 342 AA [This is the length of the unprocessed precursor]

Molecular weight: 36762 Da [This is the MW of the unprocessed precursor]

CRC64: F15CD336F1E4CFCA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVGSAKIKVG INGFGRIGRL VARVALERDD IELVAINDPF ITPEYMTYMF KYDSTHGQWK 

        70         80         90        100        110        120 
KTEVTLHSEG HLTFGGNPVA VYACRDPSEI PWGKHGADFV VESTGVFTDK DKAAAHLKGG 

       130        140        150        160        170        180 
AKKVVISAPS KDAPMFVMGV NENKYSDEDI VSNASCTTNC LAPLAKVIND KFGILEGLMT 

       190        200        210        220        230        240 
TVHATTATQK TVDGPSSKDW RGGRSAATNI IPSATGAAKA VGKVLPELNG KLTGMAFRVP 

       250        260        270        280        290        300 
TTDVSVVDLT VRLEKPASYD AIKTAIKEAS EGQMKGILGY TEDDVVSTDF ITDSRSSIFD 

       310        320        330        340 
AKAGIALSDT FVKLVAWYDN EWGYSNRVVD LIVHMAKQGT SQ

P34923 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