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Protein

Glutamate dehydrogenase 2

Gene

gdhA-2

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei109 – 1091PROSITE-ProRule annotation

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-1784-MONOMER.
SABIO-RKP80053.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2 (EC:1.4.1.3)
Short name:
GDH-2
Gene namesi
Name:gdhA-2
Synonyms:gdhA
Ordered Locus Names:SSO1907
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 420419Glutamate dehydrogenase 2PRO_0000182761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylmethionine1 Publication
Modified residuei254 – 2541N6-methyllysine1 Publication
Modified residuei260 – 2601N6-methyllysine1 Publication
Modified residuei372 – 3721N6-methyllysine1 Publication
Modified residuei391 – 3911N6-methyllysine1 Publication
Modified residuei392 – 3921N6-methyllysine1 Publication

Post-translational modificationi

Methylation of lysine residues may play a role in the thermal stability of this enzyme.

Keywords - PTMi

Acetylation, Methylation

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi273057.SSO1907.

Structurei

3D structure databases

ProteinModelPortaliP80053.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
InParanoidiP80053.
KOiK00261.
OMAiIACTRIL.

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.

P80053-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMEEVLSSSL YTQQVKKLYK VGELLGLDNE TLETLSQPER IIQVKIQIRG
60 70 80 90 100
SDGKLKTFMG WRSQHNSALG PYKGGVRYHP NVTQDEVEAL SMIMTWKNSL
110 120 130 140 150
LLLPYGGGKG GVRVDPKKLT REELEQLSRK YIQAIYKYLG SELDIPAPDV
160 170 180 190 200
NTDSQTMAWF LDEYIKITGK VDFAVFTGKP VELGGIGVRL YSTGLGVATI
210 220 230 240 250
AKEAANKFIG GVEEARVIIQ GFGNVGYYAG KFLSEMGAKI VGVSDSKGGV
260 270 280 290 300
INEKGIDVGK AIEIKEKTGS VINYPEGRKV TNEELLISDC DILIPAALEN
310 320 330 340 350
VINKFNAPKV KAKLIVEGAN GPLTADADEI MRQRGIAVVP DILANAGGVV
360 370 380 390 400
GSYVEWANNK MGEIISDEEA KKLIVDRMNN AFNTLYDYHQ KKLEDHDLRT
410 420
AAMALAVDRV VRAMKARGIL
Length:420
Mass (Da):46,031
Last modified:March 18, 2008 - v3
Checksum:iD9283C66D305EED5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031E → EE AA sequence (PubMed:1730244)Curated
Sequence conflicti392 – 3921K → KK AA sequence (PubMed:1730244)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK42099.1.
PIRiD90355.
S20286.
RefSeqiNP_343309.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42099; AAK42099; SSO1907.
GeneIDi1453426.
KEGGisso:SSO1907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK42099.1.
PIRiD90355.
S20286.
RefSeqiNP_343309.1. NC_002754.1.

3D structure databases

ProteinModelPortaliP80053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO1907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK42099; AAK42099; SSO1907.
GeneIDi1453426.
KEGGisso:SSO1907.

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
InParanoidiP80053.
KOiK00261.
OMAiIACTRIL.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-1784-MONOMER.
SABIO-RKP80053.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-epsilon-methyllysine related to thermostability?"
    Maras B., Consalvi V., Chiaraluce R., Politi L., de Rosa M., Bossa F., Scandurra R., Barra D.
    Eur. J. Biochem. 203:81-87(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-420, ACETYLATION AT MET-2, METHYLATION AT LYS-254; LYS-260; LYS-372; LYS-391 AND LYS-392.
    Strain: DSM 5833 / MT-4.

Entry informationi

Entry nameiDHE2_SULSO
AccessioniPrimary (citable) accession number: P80053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 18, 2008
Last modified: February 4, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.