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A0PNJ1 (ADD_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:
Adenosine deaminase

EC=3.5.4.4
Alternative name(s):
Adenosine aminohydrolase
Gene names
Name:add
Ordered Locus Names:MUL_1364
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Adenosine + H2O = inosine + NH3. HAMAP MF_00540

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00540

Sequence similarities

Belongs to the adenosine and AMP deaminases family. Adenosine deaminase 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 functionadenosine 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 – 362362Adenosine deaminase HAMAP MF_00540
PRO_1000017674

Sites

Active site2111Proton donor By similarity
Metal binding191Zinc; catalytic By similarity
Metal binding211Zinc; catalytic By similarity
Metal binding2081Zinc; catalytic By similarity
Metal binding3001Zinc; catalytic By similarity
Binding site211Substrate By similarity
Binding site231Substrate By similarity
Binding site1811Substrate; via amide nitrogen and carbonyl oxygen By similarity
Site2321Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PNJ1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: A1039919243D82F5

FASTA36239,739
        10         20         30         40         50         60 
MTDMPTLDAI RQAPKALLHD HLDGGLRPET VLDIAGQVGY DGLPSTDAGE LASWFRTQSH 

        70         80         90        100        110        120 
SGSLERYLEP FSHTVAVMQT PEALYRVAYE CVEDLAADAV VYAEIRFAPE LHINRGLTFD 

       130        140        150        160        170        180 
EIVDAVLAGF AAGERACAGA GCPIKVRLLV TAMRHAAMSR EIAELAIRFR DKGVVGFDIA 

       190        200        210        220        230        240 
GAEAGYPPSR HLDAFEYMRD NNARFTIHAG EAFGLPSIHE AIAFCGADRL GHGVRIVDDI 

       250        260        270        280        290        300 
EVGLDGDVKL GRLAAILRDK RIPLELCPSS NVQTGAVASI AEHPFDLLAR SRFRVTVNTD 

       310        320        330        340        350        360 
NRLMSDTSMS QEMYRLVETF GYGWSDIQRF TINAMKSAFI AFDERLEIID EVIKPRFAVL 


IG 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL03910.1.
RefSeqYP_905381.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PNJ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PNJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000073184; EBMYCP00000071189; EBMYCG00000073179.
GeneID4551961.
GenomeReviewsGene locus MUL_1364 in contig CP000325_GR.
KEGGmul:MUL_1364.
PATRIC18169578. VBIMycUlc37413_1645.

Organism-specific databases

GenoListMUL_1364.
CMRSearch...

Phylogenomic databases

eggNOGCOG1816.
GeneTreeEBGT00050000016615.
HOGENOMHBG630382.
OMAPYYMAMN.
PhylomeDBA0PNJ1.
ProtClustDBPRK09358.

Family and domain databases

HAMAPMF_00540. A_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.
PROSITEPS00485. A_DEAMINASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADD_MYCUA
AccessionPrimary (citable) accession number: A0PNJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 37 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