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Protein

NADP-specific glutamate dehydrogenase

Gene

gdh

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.By similarity

Catalytic activityi

L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Binding sitei116SubstrateBy similarity1
Active sitei128Proton donorPROSITE-ProRule annotation1
Binding sitei167Substrate; via carbonyl oxygenBy similarity1
Sitei168Important for catalysisBy similarity1
Binding sitei212NADPBy similarity1
Binding sitei243NADPBy similarity1
Binding sitei379SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11671-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-specific glutamate dehydrogenase (EC:1.4.1.4)
Short name:
NADP-GDH
Gene namesi
Name:gdh
Ordered Locus Names:Cgl2079, cg2280
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001827681 – 447NADP-specific glutamate dehydrogenaseAdd BLAST447

Proteomic databases

PRIDEiP31026.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi196627.cg2280.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 17Combined sources15
Turni18 – 20Combined sources3
Helixi22 – 41Combined sources20
Helixi43 – 49Combined sources7
Helixi50 – 54Combined sources5
Beta strandi58 – 68Combined sources11
Beta strandi74 – 85Combined sources12
Beta strandi87 – 92Combined sources6
Beta strandi95 – 97Combined sources3
Helixi103 – 119Combined sources17
Beta strandi121 – 123Combined sources3
Beta strandi126 – 132Combined sources7
Helixi140 – 154Combined sources15
Helixi155 – 157Combined sources3
Turni160 – 162Combined sources3
Helixi173 – 187Combined sources15
Helixi192 – 194Combined sources3
Turni200 – 203Combined sources4
Turni206 – 210Combined sources5
Helixi211 – 226Combined sources16
Beta strandi235 – 239Combined sources5
Helixi243 – 254Combined sources12
Beta strandi258 – 263Combined sources6
Beta strandi268 – 270Combined sources3
Helixi277 – 285Combined sources9
Helixi291 – 297Combined sources7
Beta strandi302 – 307Combined sources6
Helixi309 – 311Combined sources3
Beta strandi315 – 319Combined sources5
Helixi328 – 336Combined sources9
Beta strandi341 – 343Combined sources3
Beta strandi345 – 348Combined sources4
Helixi352 – 360Combined sources9
Beta strandi364 – 366Combined sources3
Helixi368 – 371Combined sources4
Helixi374 – 388Combined sources15
Helixi394 – 418Combined sources25
Helixi425 – 444Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IJZX-ray2.29A/B/C/D/E/F/G/H/I/J/K/L1-447[»]
ProteinModelPortaliP31026.
SMRiP31026.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107R37. Bacteria.
COG0334. LUCA.
HOGENOMiHOG000243799.
KOiK00262.
OMAiVPWVDDA.

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.

P31026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVDEQVSNY YDMLLKRNAG EPEFHQAVAE VLESLKIVLE KDPHYADYGL
60 70 80 90 100
IQRLCEPERQ LIFRVPWVDD QGQVHVNRGF RVQFNSALGP YKGGLRFHPS
110 120 130 140 150
VNLGIVKFLG FEQIFKNSLT GLPIGGGKGG SDFDPKGKSD LEIMRFCQSF
160 170 180 190 200
MTELHRHIGE YRDVPAGDIG VGGREIGYLF GHYRRMANQH ESGVLTGKGL
210 220 230 240 250
TWGGSLVRTE ATGYGCVYFV SEMIKAKGES ISGQKIIVSG SGNVATYAIE
260 270 280 290 300
KAQELGATVI GFSDSSGWVH TPNGVDVAKL REIKEVRRAR VSVYADEVEG
310 320 330 340 350
ATYHTDGSIW DLKCDIALPC ATQNELNGEN AKTLADNGCR FVAEGANMPS
360 370 380 390 400
TPEAVEVFRE RDIRFGPGKA ANAGGVATSA LEMQQNASRD SWSFEYTDER
410 420 430 440
LQVIMKNIFK TCAETAAEYG HENDYVVGAN IAGFKKVADA MLAQGVI
Length:447
Mass (Da):48,988
Last modified:July 26, 2002 - v2
Checksum:i0338926EA7080E35
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37I → L in CAA42048 (PubMed:1552846).Curated1
Sequence conflicti371 – 410ANAGG…KNIFK → TPEAVEVFRERDIRFGPGKA VNVGGVATSALEMQQNASRE in CAA42048 (PubMed:1552846).CuratedAdd BLAST40

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59404 Genomic DNA. Translation: CAA42048.2.
X72855 Genomic DNA. Translation: CAA51376.1.
BA000036 Genomic DNA. Translation: BAB99472.1.
BX927154 Genomic DNA. Translation: CAF20415.1.
PIRiS32227.
RefSeqiNP_601279.1. NC_003450.3.
WP_003856385.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99472; BAB99472; BAB99472.
CAF20415; CAF20415; cg2280.
GeneIDi1020031.
KEGGicgb:cg2280.
cgl:NCgl1999.
PATRICi21496158. VBICorGlu203724_2015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59404 Genomic DNA. Translation: CAA42048.2.
X72855 Genomic DNA. Translation: CAA51376.1.
BA000036 Genomic DNA. Translation: BAB99472.1.
BX927154 Genomic DNA. Translation: CAF20415.1.
PIRiS32227.
RefSeqiNP_601279.1. NC_003450.3.
WP_003856385.1. NC_006958.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IJZX-ray2.29A/B/C/D/E/F/G/H/I/J/K/L1-447[»]
ProteinModelPortaliP31026.
SMRiP31026.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2280.

Proteomic databases

PRIDEiP31026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99472; BAB99472; BAB99472.
CAF20415; CAF20415; cg2280.
GeneIDi1020031.
KEGGicgb:cg2280.
cgl:NCgl1999.
PATRICi21496158. VBICorGlu203724_2015.

Phylogenomic databases

eggNOGiENOG4107R37. Bacteria.
COG0334. LUCA.
HOGENOMiHOG000243799.
KOiK00262.
OMAiVPWVDDA.

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11671-MONOMER.

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_CORGL
AccessioniPrimary (citable) accession number: P31026
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 26, 2002
Last modified: November 30, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.