[1]	NUCLEOTIDE SEQUENCE [MRNA]. Chojecki J.; "Identification and characterisation of a cDNA clone for cytosolic glyceraldehyde-3-phosphate dehydrogenase in barley."; Carlsberg Res. Commun. 51:203-210(1986).

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.
MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic form which participates in glycolysis and two chloroplast forms which participates in photosynthesis. These three forms are encoded by distinct genes.
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

M36650; AAA32956.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24159; A24159.

UniGene

Hv.9630

3D structure databases

HSSP

P56649; 1DSS. [HSSP ENTRY / PDB]

ModBase

P08477.

Organism-specific databases

Gramene

P08477; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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.
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.

PROSITE

PS00071; GAPDH; PARTIAL.

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`	`<1 305`	`>305`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145603`
`REGION`	`121 123`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`181 182`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`122 122`		`Nucleophile (By similarity).`
`BINDING`	`3 3`		`NAD (By similarity).`
`BINDING`	`50 50`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`152 152`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`204 204`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`286 286`		`NAD (By similarity).`
`SITE`	`149 149`	`1`	`Activates thiol group during catalysis (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 305 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 33236 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 4F82FA362F222AC5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
VNDPFITTDY MTYMFKYDTV HGQWKHHEVK VKDSKTLLFG EKEVAVFGCR NPEEIPWAAA 

        70         80         90        100        110        120 
GAEYVVESTG VFTDKDKAAA HIKGGAKKVI ISAPSKDAPM FVCGVNEKEY KSDIDIVSNA 

       130        140        150        160        170        180 
SCTTNCPAPL AKVINDRFGI VEGLMTTVHA MTATQKTVDG PSSKDWRGGR AASFNIIPSS 

       190        200        210        220        230        240 
TGAAKAVGKV LPELNGKLTG MAFRVPTVDV SVVDLTVRLA KPATYEQIKA AIKEESEGNL 

       250        260        270        280        290        300 
KGILGYVDED LVSTDFQGDS RSSIFDAKAG IALNDNFVKL VSWYDNEWGY STRVVDLIRH 


MHSTK

P08477 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