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Protein

NAD(P)-specific glutamate dehydrogenase

Gene

gdhA

Organism
Prevotella ruminicola (Bacteroides ruminicola)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. P.ruminicola possess both NADP(H)- and NAD(H)-dependent activities on the same enzyme, suggesting that both anabolic and catabolic forms of the enzyme might occur.1 Publication

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei88SubstrateBy similarity1
Binding sitei109SubstrateBy similarity1
Binding sitei112SubstrateBy similarity1
Active sitei124Proton donorPROSITE-ProRule annotation1
Binding sitei163Substrate; via carbonyl oxygenBy similarity1
Sitei164Important for catalysisBy similarity1
Binding sitei207NADPBy similarity1
Binding sitei238NADPBy similarity1
Binding sitei376SubstrateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cellular amino acid metabolic process Source: InterPro
  • glutamate biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)-specific glutamate dehydrogenase (EC:1.4.1.2, EC:1.4.1.3)
Short name:
NAD(P)-GDH
Alternative name(s):
NAD(P)H-dependent glutamate dehydrogenase
Gene namesi
Name:gdhA
OrganismiPrevotella ruminicola (Bacteroides ruminicola)
Taxonomic identifieri839 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPrevotellaceaePrevotella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001827731 – 444NAD(P)-specific glutamate dehydrogenaseAdd BLAST444

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP95544.
SMRiP95544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd05313. NAD_bind_2_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P95544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL
60 70 80 90 100
CVPDRILQFR VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS
110 120 130 140 150
ILKFLAFEQT FKNSLTTLPM GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL
160 170 180 190 200
YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK KLTHQFQGIL TGKGLEFGGS
210 220 230 240 250
LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA QYTIEKLLQL
260 270 280 290 300
GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY
310 320 330 340 350
VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA
360 370 380 390 400
AIKVFQDAKI LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN
410 420 430 440
IMDEIHANCV KYGTEPDGYI NYVKGANVAG FMKVAKAMMA QGIY
Length:444
Mass (Da):48,878
Last modified:May 1, 1997 - v1
Checksum:i32CAD7F278CF06A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82240 Genomic DNA. Translation: AAB40142.1.
PIRiT10487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82240 Genomic DNA. Translation: AAB40142.1.
PIRiT10487.

3D structure databases

ProteinModelPortaliP95544.
SMRiP95544.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd05313. NAD_bind_2_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHE4_PRERU
AccessioniPrimary (citable) accession number: P95544
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.