[1]	NUCLEOTIDE SEQUENCE [MRNA]. Narise S., Tominaga H.; "Temperature-dependency differencies in GPDH allozmyes associated with a single base change in the coding region of the GPDH structural gene in Drosophila virilis."; Life Sci. Adv. (Genet.) 11:39-45(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0167-4781(92)90086-F; PubMed=1610907 [NCBI, ExPASy, EBI, Israel, Japan] Tominaga H., Shiba T., Narise S.; "Structure of Drosophila virilis glycerol-3-phosphate dehydrogenase gene and a comparison with the Drosophila melanogaster gene."; Biochim. Biophys. Acta 1131:233-238(1992).
[3]	PROTEIN SEQUENCE OF 2-353. Arai K., Tominaga H., Yokote Y., Narise S.; "The complete amino-acid sequence of cytoplasmic glycerol-3-phosphate dehydrogenase from Drosophila virilis."; Biochim. Biophys. Acta 953:6-13(1988).

Comments

CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD⁺ = glycerone phosphate + NADH.
PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle .
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

EMBL

X59076; CAA41800.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10697; BAA01539.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A60985; A60985.
B60985; B60985.
JS0023; JS0023.
S31790; S31790.

3D structure databases

ModBase

P07735.

Organism-specific databases

FlyBase

FBgn0013081; Dvir\Gpdh.

Ontologies

GO:0009331;	Cellular component: glycerol-3-phosphate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004367;	Molecular function: glycerol-3-phosphate dehydrogenase (NAD+) activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
GO:0046168;	Biological process: glycerol-3-phosphate catabolic process (inferred from electronic annotation from InterPro).
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

ProtoNet

P07735.

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 353`	`352`	`Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic.`	`PRO_0000138077`
`NP_BIND`	`11 16`	`6`	`NAD (By similarity).`
`REGION`	`270 271`	`2`	`Substrate binding (By similarity).`
`ACT_SITE`	`206 206`		`Proton acceptor (By similarity).`
`BINDING`	`98 98`		`NAD (By similarity).`
`BINDING`	`121 121`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`121 121`		`Substrate (By similarity).`
`BINDING`	`155 155`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`270 270`		`NAD (By similarity).`
`BINDING`	`299 299`		`NAD (By similarity).`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`
`CONFLICT`	`15 15`		`W -> N (in Ref. 3; AA sequence).`
`CONFLICT`	`35 35`		`E -> K (in Ref. 1; CAA41800).`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 38651 Da [This is the MW of the unprocessed precursor]

CRC64: E18B4DF92303D8C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEEMIDGKK LTEIINETHE 

        70         80         90        100        110        120 
NVKYLKGHKL PTNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI 

       130        140        150        160        170        180 
KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR 

       190        200        210        220        230        240 
DLFQANHFRV VVVEDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF 

       250        260        270        280        290        300 
VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEDLEK EMLNGQKLQG 

       310        320        330        340        350 
PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPKDLI DCIRNHPEHM QTL

P07735 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