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P15111 (DHE4_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADP-specific glutamate dehydrogenase

Short name=NADP-GDH
EC=1.4.1.4
Gene names
Name:gdhA
Ordered Locus Names:STM1299
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homohexamer By similarity.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamate biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutamate dehydrogenase (NADP+) activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447NADP-specific glutamate dehydrogenase
PRO_0000182776

Sites

Active site1281Proton donor By similarity
Binding site921Substrate By similarity
Binding site1131Substrate By similarity
Binding site1161Substrate By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Binding site2111NADP By similarity
Binding site2421NADP By similarity
Binding site3801Substrate By similarity
Site1681Important for catalysis By similarity

Experimental info

Sequence conflict2991E → D in AAA27131. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15111 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: CB94B38B5042E0A2

FASTA44748,574
        10         20         30         40         50         60 
MDQTCSLESF LNHVQKRDPH QTEFAQAVRE VMTTLWPFLE QNPRYRHMSL LERLVEPERV 

        70         80         90        100        110        120 
IQFRVVWLDD KNQVQVNRAW RVQFNSAIGP YKGGMRFHPS VNLSILKFLG FEQTFKNALT 

       130        140        150        160        170        180 
TLPMGGGKGG SDFDPKGKSE GEVMRFCQAL MTELYRHLGP DTDVPAGDIG VGGREVGFMA 

       190        200        210        220        230        240 
GMMRKLSNNS SCVFTGKGLS FGGSLIRPEA TGYGLVYFTE AMLKRHGLGF EGMRVAVSGS 

       250        260        270        280        290        300 
GNVAQYAIEK AMAFGARVVT ASDSSGTVVD ESGFTPEKLA RLCEIKASRD GRVADYAREF 

       310        320        330        340        350        360 
GLTYLEGQQP WSVPVDIALP CATQNELDVD AARVLIANGV KAVAEGANMP TTIEATDLFL 

       370        380        390        400        410        420 
EAGVLFAPGK AANAGGVATS GLEMAQNAAR LSWKAEKVDA RLHHIMLDIH HACVEYGGDN 

       430        440 
KHTNYVQGAN IAGFVKVADA MLAQGVI 

« Hide

References

« Hide 'large scale' references
[1]"Affinity labeling of a glutamyl peptide in the coenzyme binding site of NADP+-specific glutamate dehydrogenase of Salmonella typhimurium by 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate."
Bansal A., Dayton M.A., Zalkin H., Colman R.F.
J. Biol. Chem. 264:9827-9835(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24021 Genomic DNA. Translation: AAA27131.1.
AE006468 Genomic DNA. Translation: AAL20224.1.
PIRA33504.
RefSeqNP_460265.1. NC_003197.1.

3D structure databases

ProteinModelPortalP15111.
SMRP15111. Positions 6-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1299.

Proteomic databases

PaxDbP15111.
PRIDEP15111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20224; AAL20224; STM1299.
GeneID1252817.
KEGGstm:STM1299.
PATRIC32381075. VBISalEnt20916_1380.

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243799.
KOK00262.
OMAVAIYTIE.
OrthoDBEOG65XN4D.
ProtClustDBPRK09414.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1310-MONOMER.
SABIO-RKP15111.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. 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]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHE4_SALTY
AccessionPrimary (citable) accession number: P15111
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2002
Last modified: November 13, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families