Q9RDE5 (ADE_STRCO) 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:	SCO2546
ORF Names:	SCC77.13c

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	340 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. Ref.2
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 Reference proteome
Gene Ontology (GO)
Biological process	adenine catabolic process Inferred from genetic interaction Ref.2. Source: UniProtKB hypoxanthine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	adenine deaminase activity Inferred from genetic interaction Ref.2. Source: UniProtKB 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 – 340	340	Adenine deaminase HAMAP MF_01962		PRO_0000194389
Sites
	Active site	200	1	Proton donor By similarity
	Metal binding	17	1	Zinc; catalytic By similarity
	Metal binding	19	1	Zinc; catalytic By similarity
	Metal binding	197	1	Zinc; catalytic By similarity
	Metal binding	278	1	Zinc; catalytic By similarity
	Binding site	279	1	Substrate By similarity
	Site	221	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RDE5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 499DC13F5BFD3B80	FASTA	340	37,536
	10 20 30 40 50 60 MKRPYDALMP LPKAELHLHI EGTLEPELAF ALAARNGVSL PYADEDALRE AYRFADLQSF 70 80 90 100 110 120 LNLYYELMAV LRTERDFEDL ADAYLARAAA QGVRHAEIFF DPQAHLARGV EMGTVVEGLW 130 140 150 160 170 180 RALGASRENH GVSTRLILCF LRDESAESAM RTLDAAGPYL DRITGVGLDS AEVGHPPVKF 190 200 210 220 230 240 REVYEAAAAL GLRRVAHAGE EGPPAYVVEA LDVLGVERID HGLRSVEDPA LVERLVRERV 250 260 270 280 290 300 PLTLCPLSNV RLRTVDTLAD HPLPAMLDAG LMCTVNSDDP AYFGGYAGDN FDAVRQALGL 310 320 330 340 TGERLRELAR NSFLASFLED DEELRARYLA EVEAYRFPAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.
[2]	"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family." Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P., Scazzocchio C., Oestreicher N. J. Mol. Biol. 334:1117-1131(2003) [PubMed: 14643670] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939113 Genomic DNA. Translation: CAB66224.1.
RefSeq	NP_626784.1. NC_003888.3.
3D structure databases
ProteinModelPortal	Q9RDE5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1097980.
GenomeReviews	Gene locus SCO2546 in contig AL645882_GR.
KEGG	sco:SCO2546.
NMPDR	fig|100226.1.peg.2511.
PATRIC	23734772. VBIStrCoe124346_2591.
Phylogenomic databases
HOGENOM	HBG630382.
OMA	FGGYVDD.
PhylomeDB	Q9RDE5.
ProtClustDB	PRK09358.
Family and domain databases
HAMAP	MF_01962. Adenine_deaminase. [Tree]
InterPro	IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view]
KO	K01488.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. Aden_deam. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ADE_STRCO

Accession

Primary (citable) accession number: Q9RDE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program