ID   ADDL_STRCO              Reviewed;         343 AA.
AC   Q9L0L6;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative adenosine/adenine deaminase;
DE            EC=3.5.4.-;
DE   AltName: Full=Adenosine aminohydrolase;
GN   OrderedLocusNames=SCO4644; ORFNames=SCD82.15c;
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).
CC   -!- FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic
CC       deamination of adenosine or some similar substrate and play a role in
CC       purine metabolism (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
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DR   EMBL; AL939120; CAB77418.1; -; Genomic_DNA.
DR   RefSeq; NP_628805.1; NC_003888.3.
DR   RefSeq; WP_003974319.1; NZ_VNID01000028.1.
DR   AlphaFoldDB; Q9L0L6; -.
DR   SMR; Q9L0L6; -.
DR   STRING; 100226.SCO4644; -.
DR   DNASU; 1100085; -.
DR   GeneID; 1100085; -.
DR   KEGG; sco:SCO4644; -.
DR   PATRIC; fig|100226.15.peg.4715; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_1_11; -.
DR   InParanoid; Q9L0L6; -.
DR   OMA; RGWFRFQ; -.
DR   PhylomeDB; Q9L0L6; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01320; ADA; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A_deaminase_dom.
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.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT   CHAIN           1..343
FT                   /note="Putative adenosine/adenine deaminase"
FT                   /id="PRO_0000194390"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            228
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  37673 MW;  01C062B045E6A637 CRC64;
     MERVRDVSEL PKAHLHLHFT GSMRPTTLLE LADKHGVRLP ETLTEALGRG ESPKLRATDE
     RGWFRFQRLY DAARSCLQTP EDIQRLVREA AEEDLRDGSG WLEIQVDPTS YAPRLGGLIP
     ALEIILDAVE TTVRDTGIGM RVLVAANRMK HPLDARTLAR LAVRYAERGV VGFGLSNDER
     RGMARDFDRA FAIARDGGLL SAPHGGELTG PASVRDCLDD LEADRIGHGV RAAEDPRLLK
     RLADRQVTCE VCPASNVALG VYEKPEDVPL RRLFEAGVPM ALGADDPLLF GSRLAAQYEI
     AREHHGFTDA ELAELARQSV RGSAAPEEVK GKLLAGVDDW LVA