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Database: UniProt
Entry: A0A1S2K2J1_9ACTN
LinkDB: A0A1S2K2J1_9ACTN
Original site: A0A1S2K2J1_9ACTN 
ID   A0A1S2K2J1_9ACTN        Unreviewed;       357 AA.
AC   A0A1S2K2J1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:OII61777.1};
GN   ORFNames=BJP40_30665 {ECO:0000313|EMBL:OII61777.1};
OS   Streptomyces sp. CC53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII61777.1, ECO:0000313|Proteomes:UP000179639};
RN   [1] {ECO:0000313|EMBL:OII61777.1, ECO:0000313|Proteomes:UP000179639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC53 {ECO:0000313|EMBL:OII61777.1,
RC   ECO:0000313|Proteomes:UP000179639};
RA   Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT   "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT   transport.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OII61777.1}.
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DR   EMBL; MKXB01000170; OII61777.1; -; Genomic_DNA.
DR   RefSeq; WP_071281666.1; NZ_MKXB01000170.1.
DR   AlphaFoldDB; A0A1S2K2J1; -.
DR   STRING; 1906740.BJP40_30665; -.
DR   Proteomes; UP000179639; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:UniProt.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01320; ADA; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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   NCBIfam; TIGR01430; aden_deam; 1.
DR   PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR   PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000179639}.
FT   DOMAIN          12..337
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   357 AA;  38943 MW;  190687435CF35756 CRC64;
     MEHVVRDLKL LPKAHLHLHF TGSMRPSTLL ELADKYGVHL PEALTGGEPP KLRATDERGW
     FRFQRLYDIA RSCLREPEDI RRLVREAAEE DVRDGSGWLE IQVDPTSYAP RLGGLIPALE
     VILDAVRAAE RDTGLAIRVL VAANRMKHPL DARTLARLAV RYRDQGVVGF GLSNDERRGM
     ARDFDRAFAI ARDGGLLAAP HGGELTGPAS VRDCLDDLRA SRIGHGVRAV EDPRLLRRLA
     DRGVTCEVCP ASNVALGVYE KPEHVPLRTL FDAGVPMALG ADDPLLFGAR LADQYEIARH
     HHGFTDAELA ELARQSGRGS VAPEDVRRKL LAAIDDWLAA DPAPPGAAGS GLGRPGV
//
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