[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 30957 / WB; Rozario C., Smith M.W., Muller M.; Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-312. STRAIN=ATCC 30957 / WB; Smith M.W., Doolittle R.F.; Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.

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 (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

M88062; AAB18421.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P56649; 1CRW. [HSSP ENTRY / PDB]

ModBase

P53429.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 2.

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.

PROSITE

PS00071; GAPDH; 1.

Other

ProtoNet

P53429.

UniRef

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`	`1 337`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000145526`
`NP_BIND`	`12 13`	`2`	`NAD (By similarity).`
`REGION`	`151 153`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`211 212`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`152 152`		`Nucleophile (By similarity).`
`BINDING`	`34 34`		`NAD (By similarity).`
`BINDING`	`79 79`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`182 182`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`234 234`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`316 316`		`NAD (By similarity).`
`SITE`	`179 179`	`1`	`Activates thiol group during catalysis (By similarity).`
`VARIANT`	`214 214`	`1`	`A -> P (in strain: ATCC 30957 / WB).`
`VARIANT`	`268 268`	`1`	`N -> K (in strain: ATCC 30957 / WB).`

Sequence information

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

Molecular weight: 36450 Da [This is the MW of the unprocessed precursor]

CRC64: 762F1AE90143B462 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPIRLGINGF GRIGRMALRA SLNIDGVQVV AINDPFTDCE YMEYMLKYDT VHGRFDGTIA 

        70         80         90        100        110        120 
HSEDSITVNG NKISVFKSMK PEEIPWGKTQ VDIVLECTGR FTTKKDAELH ITGGCKRVII 

       130        140        150        160        170        180 
SAPSADAPMF VCGCNLETYD PSTMKVISNA SCTTNCLAPL AMVVNKKFGI KEGLMTTVHA 

       190        200        210        220        230        240 
VTATQLPVDG PSKKDWRGGR SCGANVIPSS TGAAKAVGKV LPALNGKLTG MAFRVPVPDV 

       250        260        270        280        290        300 
SVVDLTCTLE KDATYDEICA EIKRGSENEL KGIMTYTNED VVSSDFLSTT STCNFDSKAG 

       310        320        330 
IMLNSRFVKL VAWYDNEFGY ANKLVELAKY VGSKGCQ

P53429 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