P07735 (GPDA_DROVI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 105.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic Short name=GPD-C Short name=GPDH-C EC=1.1.1.8 | ||
| Gene names |
| ||
| Organism | Drosophila virilis (Fruit fly) | ||
| Taxonomic identifier | 7244 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › 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 | |
| Subunit structure | Homodimer. |
| Subcellular location | |
| 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 processInferred from electronic annotation. Source: InterPro glycerophospholipid metabolic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase [NAD+] activityInferred from electronic annotation. Source: EC |
| 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
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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. |
| PIR | A60985. B60985. JS0023. S31790. |
3D structure databases | |
| ProteinModelPortal | P07735. |
| SMR | P07735. Positions 1-350. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| FlyBase | FBgn0013081. Dvir\Gpdh. |
Phylogenomic databases | |
| eggNOG | COG0240. |
| InParanoid | P07735. |
| OrthoDB | EOG4G79F0. |
Enzyme and pathway databases | |
| UniPathway | UPA00086. |
Family and domain databases | |
| Gene3D | 1.10.1040.10. 1 hit. 3.40.50.720. 1 hit. |
| InterPro | IPR008927. 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] |
| PANTHER | PTHR11728. PTHR11728. 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. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
