SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54385

- DHE3_DROME

UniProt

P54385 - DHE3_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate dehydrogenase, mitochondrial

Gene
Gdh, Glud, CG5320
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381Substrate By similarity
Binding sitei162 – 1621Substrate By similarity
Binding sitei167 – 1671NAD By similarity
Active sitei174 – 1741 By similarity
Binding sitei243 – 2431NAD By similarity
Binding sitei257 – 2571GTP By similarity
Binding sitei261 – 2611GTP By similarity
Binding sitei310 – 3101GTP By similarity
Binding sitei313 – 3131GTP By similarity
Binding sitei430 – 4301Substrate By similarity
Binding sitei436 – 4361NAD By similarity
Binding sitei442 – 4421ADP By similarity
Binding sitei521 – 5211ADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 1343NAD By 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_216833. 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: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0001098. Gdh.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion Reviewed predictionAdd
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.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi67768. 22 interactions.
IntActiP54385. 1 interaction.
MINTiMINT-747345.

Structurei

3D structure databases

ProteinModelPortaliP54385.
SMRiP54385. Positions 54-562.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
InParanoidiP54385.
KOiK00261.
OMAiTCIGVIE.
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. Align

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

MYHLKSLARQ GARRQQELAT LAKALPTAVM QSSRGYATEH QIPDRLKDVP    50
TAKDPRFFDM VEYFFHRGCQ IAEESLVDDM KGKLTRDEKK QKVKGILMLM 100
QPCDHIIEIA FPLRRDAGNY EMITGYRAQH STHKTPTKGG IRFSLDVSRD 150
EVKALSALMT FKCACVDVPF GGAKAGLKIN PKEYSEHELE KITRRFTLEL 200
AKKGFIGPGV DVPAPDMGTG EREMSWIADT YAKTIGHLDI NAHACVTGKP 250
INQGGIHGRV SATGRGVFHG LENFINEANY MSQIGTTPGW GGKTFIVQGF 300
GNVGLHTTRY LTRAGATCIG VIEHDGTLYN PEGIDPKLLE DYKNEHGTIV 350
GYQNAKPYEG ENLMFEKCDI FIPAAVEKVI TSENANRIQA KIIAEAANGP 400
TTPAADKILI DRNILVIPDL YINAGGVTVS FFEWLKNLNH VSYGRLTFKY 450
ERESNYHLLA SVQQSIERII NDESVQESLE RRFGRVGGRI PVTPSESFQK 500
RISGASEKDI VHSGLDYTME RSARAIMKTA MKYNLGLDLR TAAYVNSIEK 550
IFTTYRDAGL AF 562
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei460 – 47213Missing in isoform C. VSP_001285Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 180175Missing in AAN71256. 1 PublicationAdd
BLAST
Sequence conflicti11 – 155GARRQ → APAAR in CAA72173. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi S42919.
RefSeqi NP_524470.4. NM_079746.6. [P54385-1 ]
NP_996274.1. NM_206551.3. [P54385-2 ]
UniGenei Dm.3641.

3D structure databases

ProteinModelPortali P54385.
SMRi P54385. Positions 54-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67768. 22 interactions.
IntActi P54385. 1 interaction.
MINTi MINT-747345.

Proteomic databases

PaxDbi P54385.
PRIDEi P54385.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089498 ; FBpp0088988 ; FBgn0001098 . [P54385-1 ]
GeneIDi 42832.
KEGGi dme:Dmel_CG5320.

Organism-specific databases

CTDi 42832.
FlyBasei FBgn0001098. Gdh.

Phylogenomic databases

eggNOGi COG0334.
GeneTreei ENSGT00390000000854.
InParanoidi P54385.
KOi K00261.
OMAi TCIGVIE.
OrthoDBi EOG73NG50.
PhylomeDBi P54385.

Enzyme and pathway databases

Reactomei REACT_216833. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSi GDH. drosophila.
GenomeRNAii 42832.
NextBioi 830799.
PROi P54385.

Gene expression databases

Bgeei P54385.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. 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 ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 120 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