[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 29943 / CDC 2898-73; PubMed=1955870 [NCBI, ExPASy, EBI, Israel, Japan] Lawrence J.G., Ochman H., Hartl D.L.; "Molecular and evolutionary relationships among enteric bacteria."; J. Gen. Microbiol. 137:1911-1921(1991).

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

M63363; AAA23850.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I41221; I41221.

3D structure databases

HSSP

P06977; 1DC5. [HSSP ENTRY / PDB]

SMR

P24751; 1-294.

ModBase

P24751.

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 >294`	`>294`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145659`
`REGION`	`134 136`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`194 195`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`135 135`		`Nucleophile (By similarity).`
`BINDING`	`19 19`		`NAD (By similarity).`
`BINDING`	`63 63`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`165 165`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`217 217`		`Glyceraldehyde 3-phosphate (By similarity).`
`SITE`	`162 162`	`1`	`Activates thiol group during catalysis (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`294 294`

Sequence information

Length: 294 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 31365 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 270A233457394730 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IVFRAAQKRS DIEIVAINDL LDAEYMAYML KYDSTHGRFD GTVEVKDGHL VVNGKKIRVT 

        70         80         90        100        110        120 
AERDPANLKW DEVGVDVVAE ATGIFLTDET ARKHITAGAK KVVLTGPSKD NTPMFVRGAN 

       130        140        150        160        170        180 
FDTYAGQDIV SNASCTTNCL APLAKVINDN FGIVEGLMTT VHATTATQKT VDGPSHKDWR 

       190        200        210        220        230        240 
GGRGAAQNII PSSTGAAKAV GKVLPELNGK LTGMAFRVPT PNVSVVDLTV RLEKAASYEE 

       250        260        270        280        290 
IKKAIKAASE GAMKGVLGYT EDDVVSTDFN GEVCTSVFDA KAGIALNDNF VKLV

P24751 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