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Protein

Glutamate dehydrogenase, mitochondrial

Gene

Gdh

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

Functioni

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381SubstrateBy similarity
Binding sitei162 – 1621SubstrateBy similarity
Binding sitei167 – 1671NADBy similarity
Active sitei174 – 1741PROSITE-ProRule annotation
Binding sitei243 – 2431NADBy similarity
Binding sitei257 – 2571GTPBy similarity
Binding sitei261 – 2611GTPBy similarity
Binding sitei310 – 3101GTPBy similarity
Binding sitei313 – 3131GTPBy similarity
Binding sitei430 – 4301SubstrateBy similarity
Binding sitei436 – 4361NADBy similarity
Binding sitei442 – 4421ADPBy similarity
Binding sitei521 – 5211ADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 1343NADBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate dehydrogenase (NAD+) activity Source: FlyBase
  3. glutamate dehydrogenase [NAD(P)+] activity Source: FlyBase
  4. GTP binding Source: UniProtKB-KW
  5. identical protein binding Source: FlyBase

GO - Biological processi

  1. glutamate metabolic process Source: FlyBase
  2. NADH oxidation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, GTP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_337499. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:Gdh
Synonyms:Glud
ORF Names:CG5320
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0001098. Gdh.

Subcellular locationi

  1. Mitochondrion matrix By similarity

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. cytosol Source: FlyBase
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
BLAST
Chaini54 – 562509Glutamate dehydrogenase, mitochondrialPRO_0000007214Add
BLAST

Proteomic databases

PaxDbiP54385.
PRIDEiP54385.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Expressed at all stages.1 Publication

Gene expression databases

BgeeiP54385.
ExpressionAtlasiP54385. differential.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi67768. 22 interactions.
IntActiP54385. 5 interactions.
MINTiMINT-747345.

Structurei

3D structure databases

ProteinModelPortaliP54385.
SMRiP54385. Positions 54-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
InParanoidiP54385.
KOiK00261.
OMAiFINEANY.
OrthoDBiEOG73NG50.
PhylomeDBiP54385.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. 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]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P54385-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MYHLKSLARQ GARRQQELAT LAKALPTAVM QSSRGYATEH QIPDRLKDVP
60 70 80 90 100
TAKDPRFFDM VEYFFHRGCQ IAEESLVDDM KGKLTRDEKK QKVKGILMLM
110 120 130 140 150
QPCDHIIEIA FPLRRDAGNY EMITGYRAQH STHKTPTKGG IRFSLDVSRD
160 170 180 190 200
EVKALSALMT FKCACVDVPF GGAKAGLKIN PKEYSEHELE KITRRFTLEL
210 220 230 240 250
AKKGFIGPGV DVPAPDMGTG EREMSWIADT YAKTIGHLDI NAHACVTGKP
260 270 280 290 300
INQGGIHGRV SATGRGVFHG LENFINEANY MSQIGTTPGW GGKTFIVQGF
310 320 330 340 350
GNVGLHTTRY LTRAGATCIG VIEHDGTLYN PEGIDPKLLE DYKNEHGTIV
360 370 380 390 400
GYQNAKPYEG ENLMFEKCDI FIPAAVEKVI TSENANRIQA KIIAEAANGP
410 420 430 440 450
TTPAADKILI DRNILVIPDL YINAGGVTVS FFEWLKNLNH VSYGRLTFKY
460 470 480 490 500
ERESNYHLLA SVQQSIERII NDESVQESLE RRFGRVGGRI PVTPSESFQK
510 520 530 540 550
RISGASEKDI VHSGLDYTME RSARAIMKTA MKYNLGLDLR TAAYVNSIEK
560
IFTTYRDAGL AF
Length:562
Mass (Da):62,536
Last modified:December 1, 2000 - v2
Checksum:i687A183D3BC0211F
GO
Isoform C (identifier: P54385-2) [UniParc]FASTAAdd to basket

Also known as: Short, F

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

Show »
Length:549
Mass (Da):61,082
Checksum:iE4FA8AE7638654B1
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 180175Missing in AAN71256 (PubMed:12537569).CuratedAdd
BLAST
Sequence conflicti11 – 155GARRQ → APAAR in CAA72173 (PubMed:10992165).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei460 – 47213Missing in isoform C. 1 PublicationVSP_001285Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS42919.
RefSeqiNP_524470.4. NM_079746.6. [P54385-1]
NP_996274.1. NM_206551.3. [P54385-2]
UniGeneiDm.3641.

Genome annotation databases

EnsemblMetazoaiFBtr0089498; FBpp0088988; FBgn0001098. [P54385-1]
GeneIDi42832.
KEGGidme:Dmel_CG5320.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS42919.
RefSeqiNP_524470.4. NM_079746.6. [P54385-1]
NP_996274.1. NM_206551.3. [P54385-2]
UniGeneiDm.3641.

3D structure databases

ProteinModelPortaliP54385.
SMRiP54385. Positions 54-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67768. 22 interactions.
IntActiP54385. 5 interactions.
MINTiMINT-747345.

Proteomic databases

PaxDbiP54385.
PRIDEiP54385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089498; FBpp0088988; FBgn0001098. [P54385-1]
GeneIDi42832.
KEGGidme:Dmel_CG5320.

Organism-specific databases

CTDi42832.
FlyBaseiFBgn0001098. Gdh.

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
InParanoidiP54385.
KOiK00261.
OMAiFINEANY.
OrthoDBiEOG73NG50.
PhylomeDBiP54385.

Enzyme and pathway databases

ReactomeiREACT_337499. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSiGdh. fly.
GenomeRNAii42832.
NextBioi830799.
PROiP54385.

Gene expression databases

BgeeiP54385.
ExpressionAtlasiP54385. differential.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. 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]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiDHE3_DROME
AccessioniPrimary (citable) accession number: P54385
Secondary accession number(s): P91624, Q8IH05, Q9VCF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 29, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.