NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Stackhouse;
DOI=10.1007/BF00163149; PubMed=8007000 [NCBI, ExPASy, EBI, Israel, Japan]
Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.;
"The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus.";
J. Mol. Evol. 38:319-327(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.
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

X73034; CAA51515.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X73036; CAA51517.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S43339; S43339.

3D structure databases

HSSP

P56649; 1CRW. [HSSP ENTRY / PDB]

SMR

P34920; 5-334.

ModBase

P34920.

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`	`1 335`	`335`	`Glyceraldehyde-3-phosphate dehydrogenase, cytosolic.`	`PRO_0000145597`
`NP_BIND`	`13 14`	`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`	`35 35`		`NAD (By similarity).`
`BINDING`	`80 80`		`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).`
`CONFLICT`	`250 250`		`A -> T (in Ref. 1; CAA51517).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 36054 Da [This is the MW of the unprocessed precursor]

CRC64: B09241EF399D397C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAPKVGING FGRIGRLVLR AAIEKGTCQV VAINDPFIDL DYMAYMLKYD STHGRYAGDV 

        70         80         90        100        110        120 
SIKDGKLQVD GNSITVFAHR DPAEIPWATA AADYIVEATG VFTLKDKAAA HFKGGAKKVV 

       130        140        150        160        170        180 
ISAPSKDAPM FVCGVNEAKY TPDLDIISNA SCTTNCLAPL VKVIHEKYGI EEGLMTTVHA 

       190        200        210        220        230        240 
TTATQKTVDG PSNKDWRGGR GRGRNIIPSS TGAAKAVGKV MPELNGKLTG MAFRVPTPDV 

       250        260        270        280        290        300 
SVVDLTVRLA SETTYEDIKA TMKAAADDSM KGIMKYTEDA VVSTDFIHDD ASCIFDASAG 

       310        320        330 
IMLNSKFCKL VAWYDNEWGY SNRVVDLIAH ISKVQ

P34920 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