ID   A0A318ZN47_9EURO        Unreviewed;       364 AA.
AC   A0A318ZN47;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 9.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:PYH48397.1};
GN   ORFNames=BP01DRAFT_289473 {ECO:0000313|EMBL:PYH48397.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH48397.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH48397.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH48397.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC         Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC         Evidence={ECO:0000256|ARBA:ARBA00036622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC         Evidence={ECO:0000256|ARBA:ARBA00036622};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; KZ821221; PYH48397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318ZN47; -.
DR   STRING; 1450539.A0A318ZN47; -.
DR   OrthoDB; 20281at2759; -.
DR   Proteomes; UP000248349; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   CDD; cd00443; ADA_AMPD; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF42; ADENOSINE DEAMINASE-LIKE PROTEIN; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT   DOMAIN          16..354
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   364 AA;  41116 MW;  0B3C7BE412797CE1 CRC64;
     MDLSKPVDRA FTRALPKVEL HAHLSGSISR QCLHEIWQRK KAQEPETFTI EDPLVVMPPG
     KVDYSLHTFF TTFSTMIYHL LTTLTDIRYA TYSTLTDFAA DGVTYLELRT IPRASPGHQN
     FTREEYLITV LETIAEFDRR QRGSPLETQM TTNLILAIDR GGMTAQEAME VVELAINNRR
     KCVVVGVDIC GNPTKGDISI YGPAIQKAKD AGLGVTLHFA EAQQQPQADE LMTLLDFEPD
     RLGHVIHVPG QVKEKIKKRR LALELCLSCN VHAGMVNGGF AEHHFGEWWG EKDGAVVVLC
     TDDVGFFCSP VSNEYLLAAE HFHLSRADML SLCRKSYRVI FGDSREKERL DRLLDDFEAN
     NYKR
//