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Database: UniProt
Entry: A0A1F7ZLR1_9EURO
LinkDB: A0A1F7ZLR1_9EURO
Original site: A0A1F7ZLR1_9EURO 
ID   A0A1F7ZLR1_9EURO        Unreviewed;       320 AA.
AC   A0A1F7ZLR1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=nitrilase {ECO:0000256|ARBA:ARBA00039045};
DE            EC=3.5.5.1 {ECO:0000256|ARBA:ARBA00039045};
GN   ORFNames=ABOM_010606 {ECO:0000313|EMBL:OGM40362.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40362.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM40362.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGM40362.1}.
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DR   EMBL; LYCR01000147; OGM40362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7ZLR1; -.
DR   STRING; 109264.A0A1F7ZLR1; -.
DR   OrthoDB; 2785533at2759; -.
DR   Proteomes; UP000179179; 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; PS00920; NITRIL_CHT_1; 1.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT   DOMAIN          4..283
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   ACT_SITE        44
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10139"
SQ   SEQUENCE   320 AA;  35367 MW;  3CF9E7729BCA2B37 CRC64;
     MAPVCVGTVQ AEPVFLNLDG SINKTIDIIR QAATKGVKVL AFPEVWVGGY PWPIWAKNAF
     ESSEFCAKYI AHSLPKDSTH MRRIQAACKE YSIFVVLGYS EKDDASGSIY ISQAFISFTG
     EILHNRRKIK PTYVERCLWG DGQGDSLKCV VDSPFGRIGG LNCWENLQPL LRYYEYSQGV
     QIHVAGWPSC PSVEKLEVPY PYGCTSEACL RISQMVALEG QTFVLCSTAI LSKEKHEMMG
     LKDKGIFHED DGGVAMIFGP DGRPLAEPLP RGEEGILTAV IDLEMIHAAK SLCDPVGHYS
     RPDLLSLRVN SVKAEVVHHD
//
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