Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9S1F9 (DHE4_PSYT1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 56. 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
Synonyms:gdh
OrganismPsychrobacter sp. (strain TAD1)
Taxonomic identifier81861 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. Ref.1

Catalytic activity

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

Subunit structure

Homohexamer. Ref.1

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.043 mM for NADP (at 20 degrees Celsius and at pH 8) Ref.1

KM=4 mM for ammonium (at 20 degrees Celsius and at pH 8)

KM=67.4 mM for L-glutamate (at 20 degrees Celsius and at pH 8)

pH dependence:

Optimum pH is 8.

Temperature dependence:

Optimum temperature is 25 degrees Celsius.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglutamate biosynthetic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutamate dehydrogenase (NADP+) activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 448447NADP-specific glutamate dehydrogenase
PRO_0000182774

Sites

Active site1241Proton donor By similarity
Binding site881Substrate By similarity
Binding site1091Substrate By similarity
Binding site1121Substrate By similarity
Binding site1631Substrate; via carbonyl oxygen By similarity
Binding site2071NADP By similarity
Binding site2381NADP By similarity
Binding site3751Substrate By similarity
Site1641Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S1F9 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: EE24FEA463DCB660

FASTA44849,448
        10         20         30         40         50         60 
MSISKAIEKV EARYAHQPEF IQAVKEVAIT IKPLYDAHPE YDKLKVFERL VEPDRVFGFR 

        70         80         90        100        110        120 
VNWEDDNGEI QINRGWRVQF SNALGPYKGG LRFHPTVNQS VLKFLGFEQI FKNALTGLPI 

       130        140        150        160        170        180 
GGGKGGSDFD PKGKTDSEIR RFCYAFMREL HHYVNKDMDV PAGDIGVGGR EVSYMFAMYK 

       190        200        210        220        230        240 
NLTRESTGVI TGKGVGFGGS LMRTEATGYG AVYFLQNMLA AQNESIEGKK VLVSGAGNVS 

       250        260        270        280        290        300 
LHAAEKATLI GAIVLTVSDS KGTIYDAKGL NQEKIDWLKV QKDQHKPLAD YVEVFGGEWM 

       310        320        330        340        350        360 
ADQKPWSIKA DIAIPSATQN EINEEDAKLL VDNGVKYIVE GANMPLTAEA IDYIRLHRVH 

       370        380        390        400        410        420 
YAPGKAANAG GVAVSALEMS QNSVRQYQTF EQVDERLQGI MKDIHDSSAQ ASEMYGQTDE 

       430        440 
GYIDYMSGAN MVGFKRVADA LVAFGILN 

« Hide

References

[1]"NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases."
Di Fraia R., Wilquet V., Ciardiello M.A., Carratore V., Antignani A., Camardella L., Glansdorff N., Di Prisco G.
Eur. J. Biochem. 267:121-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-448, FUNCTION AS A GLUTAMATE DEHYDROGENASE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010746 Genomic DNA. Translation: CAB54142.1.

3D structure databases

ProteinModelPortalQ9S1F9.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9S1F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PSYT1
AccessionPrimary (citable) accession number: Q9S1F9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 56 of the entry and version 4 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