ID A0A084Q7S2_STAC4 Unreviewed; 354 AA.
AC A0A084Q7S2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN ORFNames=S40285_08686 {ECO:0000313|EMBL:KFA60007.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60007.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA60007.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60007.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL661946; KFA60007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084Q7S2; -.
DR STRING; 1283841.A0A084Q7S2; -.
DR HOGENOM; CLU_039228_3_1_1; -.
DR InParanoid; A0A084Q7S2; -.
DR OMA; RPQFKPY; -.
DR OrthoDB; 20281at2759; -.
DR Proteomes; UP000028524; 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 Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 15..249
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 354 AA; 39752 MW; 26B224B093ACD772 CRC64;
MANIPVSLDF TKKLPKVELH AHLTGSISVA TLHDVWLDRK NKDPAFSLED PNIALPAEKV
SYDVFTNTES IRYATNQVLR DFEADGVRYL ELRTTPRESI PNNVTKKDYV STVLECINAF
DREKMSTYLI LSVDRRNTPA QAMETVDLAI KFKDRGVVGV DLCGNPLKGD VSLFRDAFHK
AKAAGLKITL HFAEVPESST QEELLTLLSY EPHRIGHVIN VPDNIKEAIA KKGKNIGLEL
CLSCNVHAKL IPGSFGDHHF GYWKNTECSI SICVCHVCYF LLGQRLMCIV KTDDVGIFQS
PISNEYLLIA QHFNLGRDDL IQLSQGAVDS IFSGQTEKDR MRRLLSEFRR GVDL
//
