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UniProtKB/Swiss-Prot entry Q27556


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPDA_DROAE
Primary accession number Q27556
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
Synonyms GPDH-C
GPD-C
EC 1.1.1.8
Gene name
Name: Gpdh
From
Drosophila americana (Fruit fly) [TaxID: 40366] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF01439583; PubMed=8522168 [NCBI, ExPASy, EBI, Israel, Japan]
Tominaga H., Narise S.;
"Sequence evolution of the Gpdh gene in the Drosophila virilis species group.";
Genetica 96:293-302(1995).
Comments
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
D50089; BAA20286.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q27556.
Organism-specific databases
FlyBase FBgn0015636; Dame\Gpdh.
Ontologies
GO
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.
ProtoNet Q27556.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   350  349     Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic. PRO_0000138072
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). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 38323 Da [This is the MW of the unprocessed precursor] CRC64: E23908D262F6D660 [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 VVVEDAEAVE 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 

Q27556 in FASTA format

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View entry in raw text format (no links)
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