ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P95544


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DHE4_PRERU
Primary accession number P95544
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name NAD(P)-specific glutamate dehydrogenase
Synonyms NADP-GDH
EC 1.4.1.3
NAD(P)H-dependent glutamate dehydrogenase
Gene name
Name: gdhA
From
Prevotella ruminicola (Bacteroides ruminicola) [TaxID: 839] 
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; Prevotella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B14;
PubMed=8837439 [NCBI, ExPASy, EBI, Israel, Japan]
Wen Z., Morrison M.;
"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.";
Appl. Environ. Microbiol. 62:3826-3833(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U82240; AAB40142.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T10487; T10487.
3D structure databases
HSSP P24295; 1AUP. [HSSP ENTRY / PDB]
ModBase P95544.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004353; Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from EC).
GO:0006520; Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR014362; Glu_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11606:SF2; GLFV_DH; 1.
Pfam PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000185; Glu_DH; 1.
PRINTS PR00082; GLFDHDRGNASE.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
ProtoNet P95544.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   444  444     NAD(P)-specific glutamate dehydrogenase. PRO_0000182773
ACT_SITE   124   124        By similarity. 
Sequence information
Length: 444 AA [This is the length of the unprocessed precursor] Molecular weight: 48878 Da [This is the MW of the unprocessed precursor] CRC64: 32CAD7F278CF06A9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL CVPDRILQFR 

        70         80         90        100        110        120 
VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS ILKFLAFEQT FKNSLTTLPM 

       130        140        150        160        170        180 
GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK 

       190        200        210        220        230        240 
KLTHQFQGIL TGKGLEFGGS LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA 

       250        260        270        280        290        300 
QYTIEKLLQL GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY 

       310        320        330        340        350        360 
VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA AIKVFQDAKI 

       370        380        390        400        410        420 
LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN IMDEIHANCV KYGTEPDGYI 

       430        440 
NYVKGANVAG FMKVAKAMMA QGIY 

P95544 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!