ADE_STRCO
ID ADE_STRCO Reviewed; 340 AA.
AC Q9RDE5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01962};
DE Short=ADE {ECO:0000255|HAMAP-Rule:MF_01962};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01962};
DE AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01962};
DE Short=AAH {ECO:0000255|HAMAP-Rule:MF_01962};
GN OrderedLocusNames=SCO2546; ORFNames=SCC77.13c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION.
RX PubMed=14643670; DOI=10.1016/j.jmb.2003.10.005;
RA Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P.,
RA Scazzocchio C., Oestreicher N.;
RT "Sub-families of alpha/beta barrel enzymes: a new adenine deaminase
RT family.";
RL J. Mol. Biol. 334:1117-1131(2003).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. {ECO:0000255|HAMAP-Rule:MF_01962,
CC ECO:0000269|PubMed:14643670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01962};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01962};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01962}.
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DR EMBL; AL939113; CAB66224.1; -; Genomic_DNA.
DR RefSeq; NP_626784.1; NC_003888.3.
DR RefSeq; WP_011028421.1; NC_003888.3.
DR AlphaFoldDB; Q9RDE5; -.
DR SMR; Q9RDE5; -.
DR STRING; 100226.SCO2546; -.
DR GeneID; 1097980; -.
DR KEGG; sco:SCO2546; -.
DR PATRIC; fig|100226.15.peg.2591; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_7_0_11; -.
DR InParanoid; Q9RDE5; -.
DR OMA; DERLMQR; -.
DR PhylomeDB; Q9RDE5; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IGI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IGI:UniProtKB.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..340
FT /note="Adenine deaminase"
FT /id="PRO_0000194389"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
SQ SEQUENCE 340 AA; 37536 MW; 499DC13F5BFD3B80 CRC64;
MKRPYDALMP LPKAELHLHI EGTLEPELAF ALAARNGVSL PYADEDALRE AYRFADLQSF
LNLYYELMAV LRTERDFEDL ADAYLARAAA QGVRHAEIFF DPQAHLARGV EMGTVVEGLW
RALGASRENH GVSTRLILCF LRDESAESAM RTLDAAGPYL DRITGVGLDS AEVGHPPVKF
REVYEAAAAL GLRRVAHAGE EGPPAYVVEA LDVLGVERID HGLRSVEDPA LVERLVRERV
PLTLCPLSNV RLRTVDTLAD HPLPAMLDAG LMCTVNSDDP AYFGGYAGDN FDAVRQALGL
TGERLRELAR NSFLASFLED DEELRARYLA EVEAYRFPAA
