Q7WBG5 (ADE_BORPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenine deaminase
Short name=ADE
EC=3.5.4.2

Alternative name(s):
Adenine aminohydrolase
Short name=AAH

Gene names

Ordered Locus Names:

BPP1038

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Nucleotide metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	adenine 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 317	317	Adenine deaminase HAMAP MF_01962		PRO_0000194363
Sites
	Active site	197	1	Proton donor By similarity
	Metal binding	14	1	Zinc; catalytic By similarity
	Metal binding	16	1	Zinc; catalytic By similarity
	Metal binding	194	1	Zinc; catalytic By similarity
	Metal binding	275	1	Zinc; catalytic By similarity
	Binding site	276	1	Substrate By similarity
	Site	218	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WBG5 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: B5CA6C1E18D796F0	FASTA	317	36,053
	10 20 30 40 50 60 MYDWLNALPK AELHLHLEGT LEPGLMFELA RRNGVALPWP DVESLRRAYD YDNLQEFLDL 70 80 90 100 110 120 YYRGAEVLRT EQDFYDLTWA YLLKCREQNV VHTEPFFDPQ THTDRGIAFE TVLAGITQAL 130 140 150 160 170 180 EDGRTQLGIQ GGLILSFLRH LPEEAAMRTL EQALPYRDAF IAVGLDSSER GFPPRLFQRV 190 200 210 220 230 240 FERARAAGLP AVAHAGEEGP PEYIWEALDL LQVRRIDHGV RAAEDERLIE RLIDTQIPLT 250 260 270 280 290 300 VCPLSNTRLR VFDSMAEHNI LELLERGVKV TVNSDDPAYF GGYITENFHA LHEHLGMTQD 310 QARRLAANSM DARLAGG

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640426 Genomic DNA. Translation: CAE36339.1.
RefSeq	NP_883359.1. NC_002928.3.
3D structure databases
ProteinModelPortal	Q7WBG5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1666380.
GenomeReviews	Gene locus BPP1038 in contig BX470249_GR.
KEGG	bpa:BPP1038.
PATRIC	21145710. VBIBorPar43418_1073.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG630382.
OMA	FGGYVDD.
PhylomeDB	Q7WBG5.
ProtClustDB	PRK09358.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP1038-MONOMER.
Family and domain databases
HAMAP	MF_01962. Adenine_deaminase. [Tree]
InterPro	IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view]
KO	K01488.
PANTHER	PTHR11409:SF21. PTHR11409:SF21. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. Aden_deam. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ADE_BORPA

Accession

Primary (citable) accession number: Q7WBG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program