NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1132;
DOI=10.1038/367387a0; PubMed=8114942 [NCBI, ExPASy, EBI, Israel, Japan]
Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.;
"Five identical intron positions in ancient duplicated genes of eubacterial origin.";
Nature 367:387-389(1994).

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: Algae contain three forms of GAPDH: two cytosolic forms which participate in glycolysis and one chloroplastic form 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

L27669; AAA86856.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T08147; T08147.

3D structure databases

HSSP

P06977; 1DC5. [HSSP ENTRY / PDB]

ModBase

P49644.

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`	`1 341`	`341`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145596`
`NP_BIND`	`14 15`	`2`	`NAD (By similarity).`
`REGION`	`153 155`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`213 214`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`154 154`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`184 184`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`236 236`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`318 318`		`NAD (By similarity).`
`SITE`	`181 181`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 36559 Da [This is the MW of the unprocessed precursor]

CRC64: A081514C3B13E2F7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGKIKIGIN GFGRIGRLVM RATMLRPDIE VVAINDPFID AEYMAYMFKY DSVHKTWPGH 

        70         80         90        100        110        120 
VNGSKDGFLV EGRKIHTFTE SDPSKINWGA AGADIVIEST GVFTDIAKAT AHLTGGAKKV 

       130        140        150        160        170        180 
IITAPSNDAP MYVMGVNHEK YNPATDHIIS NASCTTNCLA PLAKVVNSKF GIKEGLMTTV 

       190        200        210        220        230        240 
HATTATQKTV DGPSKKDWRG GRAVNGNIIP SSTGAAKAVG KVLPELKGKL TGMAFRVPTN 

       250        260        270        280        290        300 
DVSVVDLTVT LEKATTYEDI MKALKEASEG EMKGVLAYTD EDVVSSDFVT DPASCTVDAK 

       310        320        330        340 
AGIMLSPTFV KLVAWYDNEW GYSNRVVDLA LHVAKKAAVK V

P49644 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