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P54385 (DHE3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase, mitochondrial

Short name=GDH
EC=1.4.1.3
Gene names
Name:Gdh
Synonyms:Glud
ORF Names:CG5320
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.

Enzyme regulation

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP By similarity.

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix By similarity.

Tissue specificity

Expressed throughout the embryo during early stages before becoming localized in mesodermal tissue by stage 8. At stage 12 expression is concentrated in the posterior midgut. After stage 13 expression it is found in the anterior and posterior midgut, the hindgut, fat body, muscle, and central nervous system. In 3rd instar larvae expression is found in the leg disks, the wing pouch of the wing disk, the eye-antenna disk, and the developing brain medulla. Ref.1

Developmental stage

Expressed at all stages. Ref.1

Miscellaneous

ADP can occupy the NADH binding site and activate the enzyme By similarity.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Sequence caution

The sequence AAN71256.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P54385-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform C (identifier: P54385-2)

Also known as: Short; F;

The sequence of this isoform differs from the canonical sequence as follows:
     460-472: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Potential
Chain54 – 562509Glutamate dehydrogenase, mitochondrial
PRO_0000007214

Regions

Nucleotide binding132 – 1343NAD By similarity

Sites

Active site1741 By similarity
Binding site1381Substrate By similarity
Binding site1621Substrate By similarity
Binding site1671NAD By similarity
Binding site2431NAD By similarity
Binding site2571GTP By similarity
Binding site2611GTP By similarity
Binding site3101GTP By similarity
Binding site3131GTP By similarity
Binding site4301Substrate By similarity
Binding site4361NAD By similarity
Binding site4421ADP By similarity
Binding site5211ADP By similarity

Natural variations

Alternative sequence460 – 47213Missing in isoform C.
VSP_001285

Experimental info

Sequence conflict6 – 180175Missing in AAN71256. Ref.4
Sequence conflict11 – 155GARRQ → APAAR in CAA72173. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (Long) [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 687A183D3BC0211F

FASTA56262,536
        10         20         30         40         50         60 
MYHLKSLARQ GARRQQELAT LAKALPTAVM QSSRGYATEH QIPDRLKDVP TAKDPRFFDM 

        70         80         90        100        110        120 
VEYFFHRGCQ IAEESLVDDM KGKLTRDEKK QKVKGILMLM QPCDHIIEIA FPLRRDAGNY 

       130        140        150        160        170        180 
EMITGYRAQH STHKTPTKGG IRFSLDVSRD EVKALSALMT FKCACVDVPF GGAKAGLKIN 

       190        200        210        220        230        240 
PKEYSEHELE KITRRFTLEL AKKGFIGPGV DVPAPDMGTG EREMSWIADT YAKTIGHLDI 

       250        260        270        280        290        300 
NAHACVTGKP INQGGIHGRV SATGRGVFHG LENFINEANY MSQIGTTPGW GGKTFIVQGF 

       310        320        330        340        350        360 
GNVGLHTTRY LTRAGATCIG VIEHDGTLYN PEGIDPKLLE DYKNEHGTIV GYQNAKPYEG 

       370        380        390        400        410        420 
ENLMFEKCDI FIPAAVEKVI TSENANRIQA KIIAEAANGP TTPAADKILI DRNILVIPDL 

       430        440        450        460        470        480 
YINAGGVTVS FFEWLKNLNH VSYGRLTFKY ERESNYHLLA SVQQSIERII NDESVQESLE 

       490        500        510        520        530        540 
RRFGRVGGRI PVTPSESFQK RISGASEKDI VHSGLDYTME RSARAIMKTA MKYNLGLDLR 

       550        560 
TAAYVNSIEK IFTTYRDAGL AF 

« Hide

Isoform C (Short) (F) [UniParc].

Checksum: E4FA8AE7638654B1
Show »

FASTA54961,082

References

« Hide 'large scale' references
[1]"The glutamate dehydrogenase gene of Drosophila melanogaster: molecular analysis and expression."
Papadopoulou D., Louis C.
J. Neurogenet. 14:125-143(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS A AND C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
Strain: Berkeley.
Tissue: Embryo.
[5]"Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster."
Caggese C., De Pinto V., Ferrandino A.
Biochem. Genet. 20:449-460(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11314 mRNA. Translation: CAA72173.1.
Z29062 mRNA. Translation: CAA82304.1.
AE014297 Genomic DNA. Translation: AAF56209.5.
AE014297 Genomic DNA. Translation: AAS65200.1.
AY061323 mRNA. Translation: AAL28871.1.
BT001501 mRNA. Translation: AAN71256.1. Different initiation.
PIRS42919.
RefSeqNP_524470.4. NM_079746.6. [P54385-1]
NP_996274.1. NM_206551.3. [P54385-2]
UniGeneDm.3641.

3D structure databases

ProteinModelPortalP54385.
SMRP54385. Positions 54-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67768. 22 interactions.
IntActP54385. 1 interaction.
MINTMINT-747345.

Proteomic databases

PaxDbP54385.
PRIDEP54385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089498; FBpp0088988; FBgn0001098. [P54385-1]
GeneID42832.
KEGGdme:Dmel_CG5320.

Organism-specific databases

CTD42832.
FlyBaseFBgn0001098. Gdh.

Phylogenomic databases

eggNOGCOG0334.
GeneTreeENSGT00390000000854.
InParanoidP54385.
KOK00261.
OMATCIGVIE.
OrthoDBEOG73NG50.
PhylomeDBP54385.

Gene expression databases

BgeeP54385.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGDH. drosophila.
GenomeRNAi42832.
NextBio830799.
PROP54385.

Entry information

Entry nameDHE3_DROME
AccessionPrimary (citable) accession number: P54385
Secondary accession number(s): P91624, Q8IH05, Q9VCF7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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