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P07735 (GPDA_DROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic

Short name=GPD-C
Short name=GPDH-C
EC=1.1.1.8
Gene names
Name:Gpdh
OrganismDrosophila virilis (Fruit fly)
Taxonomic identifier7244 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophila

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 353352Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic
PRO_0000138077

Regions

Nucleotide binding11 – 166NAD By similarity
Region270 – 2712Substrate binding By similarity

Sites

Active site2061Proton acceptor By similarity
Binding site981NAD By similarity
Binding site1211NAD; via amide nitrogen By similarity
Binding site1211Substrate By similarity
Binding site1551NAD; via amide nitrogen By similarity
Binding site2701NAD By similarity
Binding site2991NAD By similarity

Amino acid modifications

Modified residue21Blocked amino end (Ala)

Experimental info

Sequence conflict151W → N AA sequence Ref.3
Sequence conflict351E → K in CAA41800. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07735 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E18B4DF92303D8C2

FASTA35338,651
        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 

« Hide

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] [Europe PMC] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59076 mRNA. Translation: CAA41800.1.
D10697 Genomic DNA. Translation: BAA01539.1.
PIRA60985.
B60985.
JS0023.
S31790.

3D structure databases

ProteinModelPortalP07735.
SMRP07735. Positions 1-350.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

FlyBaseFBgn0013081. Dvir\Gpdh.

Phylogenomic databases

eggNOGCOG0240.
InParanoidP07735.
OrthoDBEOG7ZKSBS.

Enzyme and pathway databases

UniPathwayUPA00086.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11728. PTHR11728. 1 hit.
PfamPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSPR00077. GPDHDRGNASE.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR03376. glycerol3P_DH. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPDA_DROVI
AccessionPrimary (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: November 13, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase