NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90680 / R7B;
DOI=10.1006/fgbi.2001.1313; PubMed=11860262 [NCBI, ExPASy, EBI, Israel, Japan]
Wolff A.M., Arnau J.;
"Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in Mucor circinelloides (Syn. racemosus) and use of the gpd1 promoter for recombinant protein production.";
Fungal Genet. Biol. 35:21-29(2002).

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

AJ293014; CAC37405.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00357; 4GPD. [HSSP ENTRY / PDB]

SMR

Q96UF1; 4-336.

ModBase

Q96UF1.

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`	`1 339`	`339`	`Glyceraldehyde-3-phosphate dehydrogenase 3.`	`PRO_0000145578`
`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`	`317 317`		`NAD (By similarity).`
`SITE`	`179 179`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 36302 Da [This is the MW of the unprocessed precursor]

CRC64: E64470AAABA71BC8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTINTGING FRSHWPYCLA CSLENPKVKV VAINDPFIDL EYMVYMFKYD STHGRFKGTV 

        70         80         90        100        110        120 
EHKDGKLVVN GHEIAVHAER DPAQIPWGSH GADYVIESTG VFTTKDAASA HLKGGAKKVI 

       130        140        150        160        170        180 
ISAPSADAPM FVVGVNLDKY TSDLTVISNA SCTTNCLAPL AKVIHDNYGI LEGLMTTVHA 

       190        200        210        220        230        240 
TTATQKTVDG PSNKDWRGGR GAGANIIPSS TGAAKAVGKV IPELNGKLTG MAFRVPTPDV 

       250        260        270        280        290        300 
SVVDLTVRLE KPASYDEIKA TIKKASESEE LKGILGYTED QVVSTDFVGD AHSSIFDAKA 

       310        320        330 
GIQLSPTFVK LISWYDNEFG YSTRVVDLLA YVAGKDGAL

Q96UF1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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