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P07735

- GPDA_DROVI

UniProt

P07735 - GPDA_DROVI

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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic

Gene

Gpdh

Organism
Drosophila virilis (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981NADBy similarity
Binding sitei121 – 1211NAD; via amide nitrogenBy similarity
Binding sitei121 – 1211SubstrateBy similarity
Binding sitei155 – 1551NAD; via amide nitrogenBy similarity
Active sitei206 – 2061Proton acceptorBy similarity
Binding sitei270 – 2701NADBy similarity
Binding sitei299 – 2991NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 166NADBy similarity

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycerol-3-phosphate catabolic process Source: InterPro
  3. glycerophospholipid metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00086.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (EC:1.1.1.8)
Short name:
GPD-C
Short name:
GPDH-C
Gene namesi
Name:Gpdh
OrganismiDrosophila virilis (Fruit fly)
Taxonomic identifieri7244 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophila

Organism-specific databases

FlyBaseiFBgn0013081. Dvir\Gpdh.

Subcellular locationi

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 353352Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmicPRO_0000138077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP07735.
SMRiP07735. Positions 1-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni270 – 2712Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0240.
OrthoDBiEOG7ZKSBS.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 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]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07735-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEEMIDGKK
60 70 80 90 100
LTEIINETHE NVKYLKGHKL PTNVVAVPDL VEAAKNADIL IFVVPHQFIP
110 120 130 140 150
NFCKQLLGKI KPNAIAISLI KGFDKAEGGG IDLISHIITR HLKIPCAVLM
160 170 180 190 200
GANLANEVAE GNFCETTIGC TDKKYGKVLR DLFQANHFRV VVVEDADAVE
210 220 230 240 250
VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF VDVFYPGSKL
260 270 280 290 300
STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEDLEK EMLNGQKLQG
310 320 330 340 350
PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPKDLI DCIRNHPEHM

QTL
Length:353
Mass (Da):38,651
Last modified:January 23, 2007 - v3
Checksum:iE18B4DF92303D8C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151W → N AA sequence 1 PublicationCurated
Sequence conflicti35 – 351E → K in CAA41800. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59076 mRNA. Translation: CAA41800.1.
D10697 Genomic DNA. Translation: BAA01539.1.
PIRiA60985.
B60985.
JS0023.
S31790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59076 mRNA. Translation: CAA41800.1 .
D10697 Genomic DNA. Translation: BAA01539.1 .
PIRi A60985.
B60985.
JS0023.
S31790.

3D structure databases

ProteinModelPortali P07735.
SMRi P07735. Positions 1-350.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

FlyBasei FBgn0013081. Dvir\Gpdh.

Phylogenomic databases

eggNOGi COG0240.
OrthoDBi EOG7ZKSBS.

Enzyme and pathway databases

UniPathwayi UPA00086 .

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi 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 ]
PANTHERi PTHR11728. PTHR11728. 1 hit.
Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSi PR00077. GPDHDRGNASE.
SUPFAMi SSF48179. SSF48179. 1 hit.
TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
PROSITEi PS00957. NAD_G3PDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGPDA_DROVI
AccessioniPrimary (citable) accession number: P07735
Secondary accession number(s): Q27634
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3