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A6VWL7 (ADE_MARMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:Mmwyl1_1922
OrganismMarinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]
Taxonomic identifier400668 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Marinomonas

Protein attributes

Sequence length335 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 – 335335Adenine deaminase HAMAP MF_01962
PRO_1000081925

Sites

Active site2001Proton donor By similarity
Metal binding171Zinc; catalytic By similarity
Metal binding191Zinc; catalytic By similarity
Metal binding1971Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Binding site2791Substrate By similarity
Site2211Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VWL7 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: D3BA5DC10D7E91E1

FASTA33538,033
        10         20         30         40         50         60 
METLIELSKK MPKTELHLHI EGTFEPEQMF AIAQRNQVEL KYSTVDALKA AYQFTNLQDF 

        70         80         90        100        110        120 
LDLYYQGMSV LLHEADFYDL TMAYLEKVHS ENVVHVEIFF DPQGHLSRGV GFDVQIQGIY 

       130        140        150        160        170        180 
KALQDAEKKW GMTSKLIMSF LRHLSEESAF ETLELAKPHL KWIDGIGLDS SEVGHPPEKF 

       190        200        210        220        230        240 
LRVFEACKNL GLKVTAHAGE EGPPDYVWQA IEQIGVDRID HGNRALEDNK LIEAIKQRNL 

       250        260        270        280        290        300 
TLTVCPLSNL KLCVVNDMKN HPIKNMLALG LNATVNSDDP AYFGGYMNDN YASLINGTRI 

       310        320        330 
SKEELFQLAK NGITGSWMED HLKELHLKQL HALFA

« Hide

References

[1]"Complete sequence of Marinomonas sp. MWYL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MWYL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000749 Genomic DNA. Translation: ABR70846.1.
RefSeqYP_001340781.1. NC_009654.1.

3D structure databases

ProteinModelPortalA6VWL7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VWL7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5367578.
GenomeReviewsGene locus Mmwyl1_1922 in contig CP000749_GR.
KEGGmmw:Mmwyl1_1922.
PATRIC22467205. VBIMarSp124341_1990.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHBG630382.
OMAFGGYVDD.

Enzyme and pathway databases

BioCycMSP400668:MMWYL1_1922-MONOMER.

Family and domain databases

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

Entry information

Entry nameADE_MARMS
AccessionPrimary (citable) accession number: A6VWL7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 33 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

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