ID   A0A0M9EUC2_FUSLA        Unreviewed;       337 AA.
AC   A0A0M9EUC2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:KPA39842.1};
GN   ORFNames=FLAG1_07302 {ECO:0000313|EMBL:KPA39842.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA39842.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA39842.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA39842.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
RL   Submitted (APR-2015) 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}.
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:KPA39842.1}.
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DR   EMBL; JXCE01000167; KPA39842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9EUC2; -.
DR   OrthoDB; 20281at2759; -.
DR   Proteomes; UP000037904; 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:UP000037904}.
FT   DOMAIN          7..331
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   337 AA;  37871 MW;  80DC6C5C2B7E0917 CRC64;
     MDYVELPKIE LHAHLTGSIS RQALHEIWLR KKETGNSNLG DPLVIMPEGK HDYNLQTFFP
     LFSSYIYNLI TDEESVRYTT KSVLTDFLND GVCYLELRTT PRSTPQLSAE QYIATLVDTI
     SLFESENTQL HTRLILSIDR RHTPQQAAST LELALKYRNQ GVVGLDLCGD PTARPNGDIG
     AFTPVFREAK SEGLGITVHF AEAEASGSKK ELSTLLSWEP GRLGHVIWED EETKKEIARR
     GLCLELCLSC NVRAGMVLGG FEGHHFGHWR EVEGPKISLS TDDVGVFGSP LSNEYKLVAQ
     HFGLDRQAIC ELARQPIDGI FGGDQEKERL RRLMWTQ
//