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UniProtKB/Swiss-Prot entry P54385


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

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Entry information
Entry name DHE3_DROME
Primary accession number P54385
Secondary accession numbers P91624 Q8IH05 Q9VCF7
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 71)
Name and origin of the protein
Protein name Glutamate dehydrogenase, mitochondrial [Precursor]
Synonyms GDH
EC 1.4.1.3
Gene name
Name: Gdh
Synonyms: Glud
ORFNames: CG5320
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE (ISOFORMS A AND C), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10992165 [NCBI, ExPASy, EBI, Israel, Japan]
Papadopoulou D., Louis C.;
"The glutamate dehydrogenase gene of Drosophila melanogaster: molecular analysis and expression.";
J. Neurogenet. 14:125-143(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
CHARACTERIZATION.
DOI=10.1007/BF00484696; PubMed=6810872 [NCBI, ExPASy, EBI, Israel, Japan]
Caggese C., De Pinto V., Ferrandino A.;
"Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster.";
Biochem. Genet. 20:449-460(1982).
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
Y11314; CAA72173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z29062; CAA82304.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF56209.5; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAS65200.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY061323; AAL28871.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT001501; AAN71256.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S42919; S42919.
RefSeq NP_524470.4; -.
NP_996274.1; -.
UniGene Dm.3641
3D structure databases
HSSP P00367; 1L1F. [HSSP ENTRY / PDB]
ModBase P54385.
Organism-specific databases
FlyBase FBgn0001098; Gdh.
Gene expression databases
ArrayExpress P54385; -.
GermOnline CG5320; Drosophila melanogaster.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004353; Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11606:SF2; GLFV_DH; 1.
Pfam PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00082; GLFDHDRGNASE.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
BLOCKS P54385.
Genome annotation databases
Ensembl CG5320; Drosophila melanogaster. [Contig view]
GeneID 42832; -.
KEGG dme:Dmel_CG5320; -.
NMPDR fig|7227.3.peg.14320; -.
Phylogenomic databases
HOGENOM P54385; -.
Other
ProtoNet P54385.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Complete proteome; GTP-binding; Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    53  53     Mitochondrion (Potential). 
CHAIN   54   562  509     Glutamate dehydrogenase, mitochondrial. PRO_0000007214
NP_BIND   132   134  3     NAD (By similarity). 
ACT_SITE   174   174        By similarity. 
BINDING   138   138        Substrate (By similarity). 
BINDING   162   162        Substrate (By similarity). 
BINDING   167   167        NAD (By similarity). 
BINDING   243   243        NAD (By similarity). 
BINDING   257   257        GTP (By similarity). 
BINDING   261   261        GTP (By similarity). 
BINDING   310   310        GTP (By similarity). 
BINDING   313   313        GTP (By similarity). 
BINDING   430   430        Substrate (By similarity). 
BINDING   436   436        NAD (By similarity). 
BINDING   442   442        ADP (By similarity). 
BINDING   521   521        ADP (By similarity). 
VAR_SEQ   460   472        Missing (in isoform C). VSP_001285
CONFLICT   6   180        Missing (in Ref. 4; AAN71256). 
CONFLICT   11    15        GARRQ -> APAAR (in Ref. 1; CAA72173). 
Sequence information
Length: 562 AA [This is the length of the unprocessed precursor] Molecular weight: 62536 Da [This is the MW of the unprocessed precursor] CRC64: 687A183D3BC0211F [This is a checksum on the sequence]
        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 

P54385 in FASTA format

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