ID   ADA_GIBZE               Reviewed;         353 AA.
AC   Q4IMJ1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Adenosine deaminase;
DE            EC=3.5.4.4;
DE   AltName: Full=Adenosine aminohydrolase;
GN   Name=AAH1; ORFNames=FG01567;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
CC   -!- CATALYTIC ACTIVITY: Adenosine + H(2)O = inosine + NH(3).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
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DR   EMBL; AACM01000079; EAA68522.1; -; Genomic_DNA.
DR   RefSeq; XP_381743.1; -.
DR   GeneID; 2783912; -.
DR   KEGG; fgr:FG01567.1; -.
DR   BRENDA; 3.5.4.4; 74326.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:EC.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynt...; IEA:InterPro.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006330; A_deaminase.
DR   PANTHER; PTHR11409; A/AMP_deaminase; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleotide metabolism; Nucleus.
FT   CHAIN         1    353       Adenosine deaminase.
FT                                /FTId=PRO_0000256235.
FT   ACT_SITE    208    208       Potential.
FT   ACT_SITE    256    256       Potential.
FT   ACT_SITE    289    289       Potential.
FT   ACT_SITE    290    290       Potential.
SQ   SEQUENCE   353 AA;  39774 MW;  6F9DE1537E7814F5 CRC64;
     MCKSRVHSFL QALPKVEQHL HIEGTLEPEL LFTLAEKNGI ELPNDPVYES ADKLRERYGR
     FTSLDDFLHY YYLGMSVLIT ENDFETLAYQ YFQRAAGENV RHAEIFFDPQ AHIARGVSYD
     TVVAGLVAAK HRAQKELGIT VELIVCILRH LPVPESHALV DTLLDRGHFN DGTLTGFGMV
     SSEKAFPPEL FTDVYARVAK TGTHLTTHAG EEAPPSFITA SLEHLKVSRI DHGLAAAQDP
     ELLKKLAANR TLLTFCPWSN VALCNLPELA DAPVREFLDA GVLFSVNSDD PAYFGAYVQE
     VYCRVQDTFN LSVKDWAWIV RGAVEESWCS EERKKEILKE MEQVLEKYKD LDA
//