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P95544

- DHE4_PRERU

UniProt

P95544 - DHE4_PRERU

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Protein

NAD(P)-specific glutamate dehydrogenase

Gene

gdhA

Organism
Prevotella ruminicola (Bacteroides ruminicola)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881SubstrateBy similarity
Binding sitei109 – 1091SubstrateBy similarity
Binding sitei112 – 1121SubstrateBy similarity
Active sitei124 – 1241Proton donorPROSITE-ProRule annotation
Binding sitei163 – 1631Substrate; via carbonyl oxygenBy similarity
Sitei164 – 1641Important for catalysisBy similarity
Binding sitei207 – 2071NADPBy similarity
Binding sitei238 – 2381NADPBy similarity
Binding sitei376 – 3761SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444NAD(P)-specific glutamate dehydrogenasePRO_0000182773Add
BLAST

Proteomic databases

PRIDEiP95544.

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP95544.
SMRiP95544. Positions 3-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

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:
EMBL
GenBank
DDBJ
Links Updated
U82240 Genomic DNA. Translation: AAB40142.1.
PIRiT10487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82240 Genomic DNA. Translation: AAB40142.1 .
PIRi T10487.

3D structure databases

ProteinModelPortali P95544.
SMRi P95544. Positions 3-444.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P95544.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  1. "The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth."
    Wen Z., Morrison M.
    Appl. Environ. Microbiol. 62:3826-3833(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GLUTAMATE DEHYDROGENASE, SUBSTRATE SPECIFICITY.
    Strain: B14.

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: October 1, 2014
This is version 64 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

External Data

Dasty 3