ID A1D295_NEOFI Unreviewed; 288 AA.
AC A1D295;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Adenosine deaminase, putative {ECO:0000313|EMBL:EAW22538.1};
GN ORFNames=NFIA_012270 {ECO:0000313|EMBL:EAW22538.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22538.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22538.1; -; Genomic_DNA.
DR RefSeq; XP_001264435.1; XM_001264434.1.
DR AlphaFoldDB; A1D295; -.
DR STRING; 331117.A1D295; -.
DR EnsemblFungi; EAW22538; EAW22538; NFIA_012270.
DR GeneID; 4591969; -.
DR KEGG; nfi:NFIA_012270; -.
DR VEuPathDB; FungiDB:NFIA_012270; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_3_1_1; -.
DR OMA; RPQFKPY; -.
DR OrthoDB; 20281at2759; -.
DR Proteomes; UP000006702; 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:UP000006702}.
FT DOMAIN 5..276
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 288 AA; 31936 MW; D75814CC6851478E CRC64;
MHSFFSVFSK SIYQLCNDLD SLAYATHSVL QNFLADGVRY LELRTIPRAS PTLAFTRTEY
LTTVLTTIET FLSVHSPQIS VYLILAIDRG NNTAADALSI IDLAIAHRPR VVGVDICGNP
TKGDVALYGP ALAKAKAHGL GITVHFAETQ ASGSERELST LLSFRPDRLG HVIHVPEDFK
REIARRRLGL ELCMSCNVHA EMIDGGFPAH HFGYWRHVDC PVVLCTDDMG FFCSPVSNEY
LLAAEHFDLG RAELLALCRE SVDVIFGGQA EKERMRGLLL DFEDTYTS
//
