Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0C934 (DHE2_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 22. 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:
NAD-specific glutamate dehydrogenase

Short name=NAD-GDH
EC=1.4.1.2
Alternative name(s):
Surface-associated protein PGAG1
Gene names
Name:gdh
Ordered Locus Names:PG_1232
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in degradation rather than biosynthesis of glutamate.

Catalytic activity

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

Subunit structure

Homohexamer Probable.

Subcellular location

Cell surface.

Sequence similarities

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

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglutamate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445NAD-specific glutamate dehydrogenase
PRO_0000182740

Sites

Active site1241 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C934 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 7436A9C2E01C503D

FASTA44549,199
        10         20         30         40         50         60 
MKTQEIMTML EAKHPGESEF LQAVKEVLLS VEEVYNQHPE FEKNGIIERI VEPDRVFTFR 

        70         80         90        100        110        120 
VPWVDDQGKV QVNIGYRVQF NNAIGPYKGG IRFHPSVNLS ILKFLGFEQM FKNALTTLPM 

       130        140        150        160        170        180 
GGGKGGADFS PKGKSEAEIM RFCQSFMTEL WRNIGPDTDI PAGDIGVGGR EVGYMFGMYK 

       190        200        210        220        230        240 
KLAREHTGTL TGKGFEFGGS RLRPESTGFG AVYFVQNMCK QNGVDYKGKT LAISGFGNVA 

       250        260        270        280        290        300 
WGVAQKATEL GIKVVTISGP DGYVYDPDGI NTPEKFRCML DLRDSGNDVV SDYVKRFPNA 

       310        320        330        340        350        360 
QFFPGKKPWE QKVDFAMPCA TQNEMNLEDA KTLHKNGVTL VAETSNMGCT AEASEYYVAN 

       370        380        390        400        410        420 
KMLFAPGKAV NAGGVSCSGL EMTQNAMHLV WTNEEVDKWL HQIMQDIHEQ CVTYGKDGNY 

       430        440 
IDYVKGANIA GFMKVAKAMV AQGVC 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed: 12949112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.
[2]"Characterization of recombinant and native forms of a cell surface antigen of Porphyromonas (Bacteroides) gingivalis."
Joe A., Yamamoto A., McBride B.C.
Infect. Immun. 61:3294-3303(1993) [PubMed: 8392971] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-29.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ66318.1.
RefSeqNP_905419.1. NC_002950.2.

3D structure databases

ProteinModelPortalP0C934.
SMRP0C934. Positions 3-444.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2553197.
GenomeReviewsGene locus PG_1232 in contig AE015924_GR.
KEGGpgi:PG1232.
PATRIC22979506. VBIPorGin134034_1145.
TIGRPG_1232.

Phylogenomic databases

OMAGNVAWGA.
PhylomeDBP0C934.
ProtClustDBPRK14030.

Family and domain databases

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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00262.
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 nameDHE2_PORGI
AccessionPrimary (citable) accession number: P0C934
Secondary accession number(s): Q03578
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: January 25, 2012
This is version 22 of the entry and version 1 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