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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.
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Substrate By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei112 – 1121Substrate By similarity
Active sitei124 – 1241Proton donor By similarity
Binding sitei163 – 1631Substrate; via carbonyl oxygen By similarity
Sitei164 – 1641Important for catalysis By similarity
Binding sitei207 – 2071NADP By similarity
Binding sitei238 – 2381NADP By similarity
Binding sitei376 – 3761Substrate By 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 dehydrogenase
PRO_0000182773Add
BLAST

Proteomic databases

PRIDEiP95544.

Interactioni

Subunit structurei

Homohexamer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP95544.
SMRiP95544. Positions 3-444.

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

MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL    50
CVPDRILQFR VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS 100
ILKFLAFEQT FKNSLTTLPM GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL 150
YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK KLTHQFQGIL TGKGLEFGGS 200
LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA QYTIEKLLQL 250
GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY 300
VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA 350
AIKVFQDAKI LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN 400
IMDEIHANCV KYGTEPDGYI NYVKGANVAG FMKVAKAMMA QGIY 444
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 16, 2013
This is version 63 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

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