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Database: UniProt
Entry: A1DAM8_NEOFI
LinkDB: A1DAM8_NEOFI
Original site: A1DAM8_NEOFI 
ID   A1DAM8_NEOFI            Unreviewed;       318 AA.
AC   A1DAM8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=nitrilase {ECO:0000256|ARBA:ARBA00039045};
DE            EC=3.5.5.1 {ECO:0000256|ARBA:ARBA00039045};
GN   ORFNames=NFIA_095380 {ECO:0000313|EMBL:EAW19918.1};
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:EAW19918.1, 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=a nitrile + 2 H2O = a carboxylate + NH4(+);
CC         Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036406};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000256|ARBA:ARBA00008129}.
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DR   EMBL; DS027694; EAW19918.1; -; Genomic_DNA.
DR   RefSeq; XP_001261815.1; XM_001261814.1.
DR   AlphaFoldDB; A1DAM8; -.
DR   STRING; 331117.A1DAM8; -.
DR   EnsemblFungi; EAW19918; EAW19918; NFIA_095380.
DR   GeneID; 4588848; -.
DR   KEGG; nfi:NFIA_095380; -.
DR   VEuPathDB; FungiDB:NFIA_095380; -.
DR   eggNOG; KOG0805; Eukaryota.
DR   HOGENOM; CLU_030130_6_0_1; -.
DR   OMA; AWLYHET; -.
DR   OrthoDB; 2785533at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0000257; F:nitrilase activity; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07564; nitrilases_CHs; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
DR   InterPro; IPR044149; Nitrilases_CHs.
DR   PANTHER; PTHR46044:SF1; CN HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46044; NITRILASE; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT   DOMAIN          4..280
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   318 AA;  34983 MW;  0128753F0EEBD4A5 CRC64;
     MTKVRVGAVQ AEPAWNDLQG GVAKTIKLIK EAGEKGINVL GFPEVWIPGY LWSMWTNSPI
     DNVQLFHEYM ANSLARNSPE MDAIRAAVKE AGIFIVLGYS ERDAGSIYMA QSFISPEGEI
     VHHRRKLKPT HVERCIWGES QADSLKTVVD SPFGKIGALN CWEHLQPLLR YYEYEQGAQI
     HVASWPAMFP MVKSVPWGFS ATGAGCQLMS QFMAIEGQTF VLACTQILTK ENLAKQNLVE
     EGIIQVPGGG FAMIFGPDGT PLVEAPPPGV ECILQADIDL QHIDYAKALA DPVGHYSRPD
     LLQLKVNKTA AKCVVDME
//
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