[1]	NUCLEOTIDE SEQUENCE [MRNA]. Hausmann L., Schell J., Toepfer R.; "Cloning of a cDNA coding for a glycerol-3-phosphate dehydrogenase from Cuphea lanceolata."; (In) Kader J.-C., Mazliak P. (eds.); Plant lipid metabolism, pp.534-536, Kluwer Academic Publishers, Dordrecht (1995).

Comments

CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD⁺ = glycerone phosphate + NADH.
SIMILARITY: Belongs to the NAD-dependent glycerol-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

X79677; CAA56125.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P52425.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

PANTHER

PTHR11728; NAD_Gly3P_DH; 1.

Pfam

PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000114; Glycerol-3-P_dh; 1.

PRINTS

PR00077; GPDHDRGNASE.

ProDom

PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00957; NAD_G3PDH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 372`	`372`	`Glycerol-3-phosphate dehydrogenase [NAD+].`	`PRO_0000138071`
`NP_BIND`	`29 34`	`6`	`NAD (By similarity).`
`REGION`	`289 290`	`2`	`Substrate binding (By similarity).`
`ACT_SITE`	`225 225`		`Proton acceptor (By similarity).`
`BINDING`	`117 117`		`NAD (By similarity).`
`BINDING`	`140 140`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`140 140`		`Substrate (By similarity).`
`BINDING`	`173 173`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`289 289`		`NAD (By similarity).`
`BINDING`	`320 320`		`NAD (By similarity).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 40811 Da [This is the MW of the unprocessed precursor]

CRC64: 1BF91793CDC23AA9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPSELNCTH QNQHSSGYDG PRSRVTVVGS GNWGSVAAKL IATNTLKLPS FHDEVRMWVF 

        70         80         90        100        110        120 
EETLPSGEKL TDVINQTNEN VKYLPGIKLG RNVVADPDLE NAVKDANMLV FVTPHQFMEG 

       130        140        150        160        170        180 
ICKRLEGKIQ EGAQALSLIK GMEVKMEGPC MISSLISDLL GINCCVLMGA NIANEIAVEK 

       190        200        210        220        230        240 
FSEATVGFRE NRDIAEKWVQ LFSTPYFMVS AVEDVEGVEL CGTLKNIVAI AAGFVDGLEM 

       250        260        270        280        290        300 
GNNTKAAIMR IGLREMKAFS KLLFPSVKDT TFFESCGVAD LITTCLGGRN RKVAEAFAKN 

       310        320        330        340        350        360 
GGKRSFDDLE AEMLRGQKLQ GVSTAKEVYE VLGHRGWLEL FPLFSTVHEI STGRLPPSAI 

       370 
VEYSEQKTIF SW

P52425 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