Reviewed, UniProtKB/Swiss-Prot P07735 (GPDA_DROVI)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
      Short name=GPDH-C
      Short name=GPD-C
    EC=1.1.1.8

Gene names

Name:

Gpdh

Organism

Drosophila virilis (Fruit fly)

Taxonomic identifier

7244 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.
Pathway	Phospholipid metabolism; alpha-glycerophosphate cycle.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 353	352	Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic		PRO_0000138077
Regions
	Nucleotide binding	11 – 16	6	NAD By similarity
	Region	270 – 271	2	Substrate binding By similarity
Sites
	Active site	206	1	Proton acceptor By similarity
	Binding site	98	1	NAD By similarity
	Binding site	121	1	NAD; via amide nitrogen By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	155	1	NAD; via amide nitrogen By similarity
	Binding site	270	1	NAD By similarity
	Binding site	299	1	NAD By similarity
Amino acid modifications
	Modified residue	2	1	Blocked amino end (Ala)
Experimental info
	Sequence conflict	15	1	W → N AA sequence Ref.3
	Sequence conflict	35	1	E → K in CAA41800. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07735-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E18B4DF92303D8C2	FASTA	353	38,651
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59076 mRNA. Translation: CAA41800.1. D10697 Genomic DNA. Translation: BAA01539.1.
PIR	A60985. B60985. JS0023. S31790.
3D structure databases
ModBase	Search...
Organism-specific databases
FlyBase	FBgn0013081. Dvir\Gpdh.
Enzyme and pathway databases
BRENDA	1.1.1.8. 141708.
Family and domain databases
InterPro	IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006168. NAD-dep_Gly3P_DH. IPR017751. NAD-dep_Gly3P_DH_euk. IPR011128. NAD-dep_Gly3P_DH_N. IPR006109. NAD_Gly3P_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR11728. NAD_Gly3P_DH. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
ProDom	PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03376. glycerol3P_DH. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPDA_DROVI

Accession

Primary (citable) accession number: P07735
Secondary accession number(s): Q27634

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project