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Q54KB7

- DHE3_DICDI

UniProt

Q54KB7 - DHE3_DICDI

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Protein

Glutamate dehydrogenase, mitochondrial

Gene

gluD

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 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 AMP and ADP.2 Publications

Kineticsi

  1. KM=0.36 mM for alpha-ketoglutarate1 Publication
  2. KM=16 µM for NADH1 Publication
  3. KM=34.5 mM for NH31 Publication

pH dependencei

Optimum pH is 7.25 to 7.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei102 – 1021SubstrateBy similarity
Binding sitei126 – 1261SubstrateBy similarity
Binding sitei131 – 1311NADBy similarity
Active sitei138 – 1381PROSITE-ProRule annotation
Binding sitei394 – 3941SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 983NADBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate dehydrogenase [NAD(P)+] activity Source: dictyBase

GO - Biological processi

  1. glutamate catabolic process Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ54KB7.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:gluD
ORF Names:DDB_G0287469
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 5, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0287469. glud1.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: dictyBase
  2. phagocytic vesicle Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 502Glutamate dehydrogenase, mitochondrialPRO_0000327666
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PRIDEiQ54KB7.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB_0231438.

Structurei

3D structure databases

ProteinModelPortaliQ54KB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
InParanoidiQ54KB7.
KOiK00261.
OMAiTMELCQK.
PhylomeDBiQ54KB7.

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.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q54KB7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSLARLSRT SLVQKGLVPQ TIKNYSSVSQ AEIDNEPRFL ECFKTFFDKA
60 70 80 90 100
AGLTNLKPGV LNNMKECNVA LRVEFPIKNE HGDVDIIAGY RAQHSHHRLP
110 120 130 140 150
CKGGIRFSEE VDLQEVMALA SLMTYKCAVV DVPFGGAKGG VRIDPKKYTV
160 170 180 190 200
AQREKITRAY TLLLCQKNFI GPGVDVPAPD MGTGEQEMAW IRDTYQAFNT
210 220 230 240 250
NDVDSMACVT GKPISSGGIR GRTEATGLGV FYGIREFLSY EEVLKKTGLT
260 270 280 290 300
PGIKGKSIVI QGFGNVGYFA AKFFEQAGAK VIAVAEHNGA VYNADGLNID
310 320 330 340 350
ALNKYKLQHG TFIDFPGATN IVDSVKALEI PCDILIPAAL EKQIHIGNVA
360 370 380 390 400
DIQAKLIGEA ANGPMTPRAD QILLNRGHVI IPDLLLNAGG VTVSYFEWLK
410 420 430 440 450
NLSHVRFGRL NKKWEESSKK LLLEFVESTV NKKLSEAERS LIIHGADEID
460 470 480 490 500
IVRSGLEDTM QNACAETRKT ANEKNTDYRS AALYNAIMKI KAVYESSGNV

FS
Length:502
Mass (Da):55,042
Last modified:May 24, 2005 - v1
Checksum:iD6BB324A859C0528
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000101 Genomic DNA. Translation: EAL63700.1.
RefSeqiXP_637204.1. XM_632112.1.

Genome annotation databases

EnsemblProtistsiDDB0231438; DDB0231438; DDB_G0287469.
GeneIDi8626141.
KEGGiddi:DDB_G0287469.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000101 Genomic DNA. Translation: EAL63700.1 .
RefSeqi XP_637204.1. XM_632112.1.

3D structure databases

ProteinModelPortali Q54KB7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 44689.DDB_0231438.

Proteomic databases

PRIDEi Q54KB7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi DDB0231438 ; DDB0231438 ; DDB_G0287469 .
GeneIDi 8626141.
KEGGi ddi:DDB_G0287469.

Organism-specific databases

dictyBasei DDB_G0287469. glud1.

Phylogenomic databases

eggNOGi COG0334.
InParanoidi Q54KB7.
KOi K00261.
OMAi TMELCQK.
PhylomeDBi Q54KB7.

Enzyme and pathway databases

SABIO-RK Q54KB7.

Miscellaneous databases

PROi Q54KB7.

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.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000185. Glu_DH. 1 hit.
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 genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties."
    Pamula F., Wheldrake J.F.
    Arch. Biochem. Biophys. 291:225-230(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  3. "The effect of AMP on the NAD-dependent glutamate dehydrogenase during activation and morphogenesis in the cellular slime moulds."
    Pamula F., Wheldrake J.F.
    J. Gen. Microbiol. 138:1935-1940(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiDHE3_DICDI
AccessioniPrimary (citable) accession number: Q54KB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: October 29, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3