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Q87GM3 (ADE_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:
Adenine deaminase

Short name=ADE
EC=3.5.4.2
Alternative name(s):
Adenine aminohydrolase
Short name=AAH
Gene names
Ordered Locus Names:VPA1292
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism By similarity. HAMAP MF_01962

Catalytic activity

Adenine + H2O = hypoxanthine + NH3. HAMAP MF_01962

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01962

Sequence similarities

Belongs to the adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionadenine deaminase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Adenine deaminase HAMAP MF_01962
PRO_0000194399

Sites

Active site1971Proton donor By similarity
Metal binding141Zinc; catalytic By similarity
Metal binding161Zinc; catalytic By similarity
Metal binding1941Zinc; catalytic By similarity
Metal binding2751Zinc; catalytic By similarity
Binding site2761Substrate By similarity
Site2181Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87GM3 [UniParc].

Last modified May 30, 2003. Version 1.
Checksum: FC6A2B523742F3BF

FASTA33737,998
        10         20         30         40         50         60 
MNAFIQGLPK VELHLHIEGS LEPELMFKLA KRNGIDIPYS SPSELREAYQ FEDLQSFLDL 

        70         80         90        100        110        120 
YYQGANVLRT EQDFYDLTWE YLEHCKADNV IHTEIFFDPQ THTERGIDFD TVLNGISRAL 

       130        140        150        160        170        180 
TDGREKLGIT SQIIACFLRH LSEESAMETL QSVLKHRDKI IGVGLDSSEK GHPPAKFLRV 

       190        200        210        220        230        240 
FQQAKEAGLL TVAHAGEEGP AQNITDAIEM LEVSRVDHGV RCVEDEALVG SLIETKMPLT 

       250        260        270        280        290        300 
VCPLSNIKLC VFDEMGQHNI VELLRKGVAV TINSDDPVYF GGYMTDNFLA VNQAHPMIKE 

       310        320        330 
ELAKFTLNAI DASFIDNELK AQYRHKVEQY VAQHSSM 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000032 Genomic DNA. Translation: BAC62635.1.
RefSeqNP_800802.1. NC_004605.1.

3D structure databases

ProteinModelPortalQ87GM3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1191988.
GenomeReviewsGene locus VPA1292 in contig BA000032_GR.
KEGGvpa:VPA1292.
NMPDRfig|223926.1.peg.4372.
PATRIC20146983. VBIVibPar50997_4218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG630382.
OMAENFHALY.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycVPAR223926:VPA1292-MONOMER.

Family and domain databases

HAMAPMF_01962. Adenine_deaminase.
[Tree]
InterProIPR001365. A/AMP_deaminase_dom.
IPR006330. A_deaminase.
[Graphical view]
KOK01488.
PANTHERPTHR11409:SF21. PTHR11409:SF21. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01430. Aden_deam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameADE_VIBPA
AccessionPrimary (citable) accession number: Q87GM3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
Last modified: January 25, 2012
This is version 50 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