ID A0A165GQ72_EXIGL Unreviewed; 343 AA.
AC A0A165GQ72;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Metallo-dependent hydrolase {ECO:0000313|EMBL:KZV90846.1};
GN ORFNames=EXIGLDRAFT_710662 {ECO:0000313|EMBL:KZV90846.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90846.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90846.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90846.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426039; KZV90846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GQ72; -.
DR STRING; 1314781.A0A165GQ72; -.
DR InParanoid; A0A165GQ72; -.
DR OrthoDB; 20281at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0019239; F:deaminase activity; IEA:InterPro.
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 Hydrolase {ECO:0000313|EMBL:KZV90846.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 27..332
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 343 AA; 37595 MW; 6A427E172A39C399 CRC64;
MNDIAGPAAA ALASLKRYER VFISLLPKAE LHAHLNGCIP LDCLRELARD YAPEPGEPTV
DLTAFADGIK LDEIHDFFKL FPAIYALTAT PAALRVATRA VLDQFIGDDA RQQNCAYVEL
RTTPRTTKHM TRKEYLEAVL DEVELSPKDR TALLVAVDRR MEESVVAEIV NLAIELKNAG
RRVVGMDLCG EPLAGDVHML VKHLARAKEA GLGVTVHVAE TSANTAEDTM ALLSFEPTRL
GHATFLNDEA RAFVEEHRIP IEICLTSNLL CKTVSALEDH HIKHWLLRDH PVAICTDDTL
PFRTSLAGEY ALLLAKPPLG LGLSEDEVSA IAERGLGARM GQM
//
