[1]	SECONDARY STRUCTURE PREDICTION. PubMed=6773774 [NCBI, ExPASy, EBI, Israel, Japan] Otto J., Argos P., Rossmann M.G.; "Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases."; Eur. J. Biochem. 109:325-330(1980).

Comments

CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD⁺ = glycerone phosphate + NADH.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
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
PIR	A32512; A32512.
3D structure databases
HSSP	P90551; 1EVY. [HSSP ENTRY / PDB]
ModBase	P08507.
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.
BLOCKS	P08507.
Phylogenomic databases
HOVERGEN	P08507; -.
Other
ProtoNet	P08507.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 349`	`348`	`Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic.`	`PRO_0000138081`
`NP_BIND`	`10 15`	`6`	`NAD (By similarity).`
`REGION`	`269 270`	`2`	`Substrate binding (By similarity).`
`ACT_SITE`	`204 204`		`Proton acceptor (By similarity).`
`BINDING`	`97 97`		`NAD (By similarity).`
`BINDING`	`120 120`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`120 120`		`Substrate (By similarity).`
`BINDING`	`153 153`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`269 269`		`NAD (By similarity).`
`BINDING`	`298 298`		`NAD (By similarity).`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 37610 Da [This is the MW of the unprocessed precursor]

CRC64: A11FE0E1F4ADD807 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGKKVCIVG SGDWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTHQEN 

        70         80         90        100        110        120 
VKYLPGHKLP PNVVAVPDVV KAAADADILI FVVPHQFIGK ICDEIKGHLK ANAIGISLIK 

       130        140        150        160        170        180 
GVNEGPKGLK LISEVIGEHL GIPMSVLMGA NIASEVADEK FCETTIGCKD QAQGQLLKQL 

       190        200        210        220        230        240 
MQTPNFRIVV TQEVNTVEIC GALKDLVAVG AGFCDGIGFG DNTKAAVIRL GLMEMIAFAK 

       250        260        270        280        290        300 
LFCSGPVSPA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP 

       310        320        330        340 
ETARELHSIL QHKGLVDWFP LFMAVYKVCY QGQPVGEFIR CLQNHPEHM

P08507 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