Reviewed, UniProtKB/Swiss-Prot P54385 (DHE3_DROME)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase, mitochondrial
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	Gdh
Synonyms:	Glud
ORF Names:	CG5320

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + 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 matrixBy 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.
Developmental stage	Expressed at all stages.
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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	ATP-binding GTP-binding NAD Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 53	53	Mitochondrion Potential
	Chain	54 – 562	509	Glutamate dehydrogenase, mitochondrial		PRO_0000007214
Regions
	Nucleotide binding	132 – 134	3	NAD By similarity
Sites
	Active site	174	1	By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	162	1	Substrate By similarity
	Binding site	167	1	NAD By similarity
	Binding site	243	1	NAD By similarity
	Binding site	257	1	GTP By similarity
	Binding site	261	1	GTP By similarity
	Binding site	310	1	GTP By similarity
	Binding site	313	1	GTP By similarity
	Binding site	430	1	Substrate By similarity
	Binding site	436	1	NAD By similarity
	Binding site	442	1	ADP By similarity
	Binding site	521	1	ADP By similarity
Natural variations
	Alternative sequence	460 – 472	13	Missing in isoform C.		VSP_001285
Experimental info
	Sequence conflict	6 – 180	175	Missing in AAN71256. Ref.4
	Sequence conflict	11 – 15	5	GARRQ → APAAR in CAA72173. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Long) [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 687A183D3BC0211F	FASTA	562	62,536
	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
	Isoform C (Short) (F) [UniParc]. Checksum: E4FA8AE7638654B1		549	61,082
	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 ERESNYHLLE SVQESLERRF GRVGGRIPVT 490 500 510 520 530 540 PSESFQKRIS GASEKDIVHS GLDYTMERSA RAIMKTAMKY NLGLDLRTAA YVNSIEKIFT TYRDAGLAF

References

	« Hide 'large scale' referencesShow '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: 10992165] [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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[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: 12537569] [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: 6810872] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	S42919.
RefSeq	NP_524470.4. NP_996274.1.
UniGene	Dm.3641
3D structure databases
HSSP	HSSP built from PDB template 1L1F based on UniProtKB P00367.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54385.
Genome annotation databases
Ensembl	CG5320. Drosophila melanogaster. [Contig view]
GeneID	42832.
KEGG	dme:Dmel_CG5320.
NMPDR	fig|7227.3.peg.14320.
Organism-specific databases
FlyBase	FBgn0001098. Gdh.
Phylogenomic databases
HOGENOM	P54385.
Gene expression databases
ArrayExpress	P54385.
GermOnline	CG5320. Drosophila melanogaster.
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11606:SF2. GLFV_DH. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PRINTS	PR00082. GLFDHDRGNASE.
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	830799.

Entry information

Entry name

DHE3_DROME

Accession

Primary (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:	November 25, 2008
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project