ID   NIT_MACPH               Reviewed;         344 AA.
AC   K2QXC4; A0A0P1DJB9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:26521240};
DE            EC=3.5.5.1 {ECO:0000269|PubMed:26521240};
DE            EC=3.5.5.5 {ECO:0000269|PubMed:26521240};
DE   AltName: Full=NitMp {ECO:0000303|PubMed:26521240};
GN   ORFNames=MPH_08355;
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=26521240; DOI=10.1007/s00253-015-7023-1;
RA   Vesela A.B., Rucka L., Kaplan O., Pelantova H., Nesvera J., Patek M.,
RA   Martinkova L.;
RT   "Bringing nitrilase sequences from databases to life: the search for novel
RT   substrate specificities with a focus on dinitriles.";
RL   Appl. Microbiol. Biotechnol. 100:2193-2202(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6;
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile
CC       and (R,S)-mandelonitrile. Also acts on dinitriles like
CC       phenylenediacetonitriles (PDAs) 1,2-PDA, 1,3-PDA, and 1,4-PDA, and
CC       cyanophenyl acetonitriles (CPAs) 2-CPA and 4-CPA.
CC       {ECO:0000269|PubMed:26521240}.
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:0000269|PubMed:26521240};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate +
CC         NH4(+); Xref=Rhea:RHEA:20657, ChEBI:CHEBI:15377, ChEBI:CHEBI:16237,
CC         ChEBI:CHEBI:17346, ChEBI:CHEBI:28938; EC=3.5.5.5;
CC         Evidence={ECO:0000269|PubMed:26521240};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; LN875497; CTQ87321.1; -; Genomic_DNA.
DR   EMBL; AHHD01000347; EKG14506.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2QXC4; -.
DR   SMR; K2QXC4; -.
DR   STRING; 1126212.K2QXC4; -.
DR   EnsemblFungi; EKG14506; EKG14506; MPH_08355.
DR   eggNOG; KOG0805; Eukaryota.
DR   HOGENOM; CLU_030130_6_0_1; -.
DR   InParanoid; K2QXC4; -.
DR   OrthoDB; 996578at2759; -.
DR   BRENDA; 3.5.5.5; 3139.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047428; F:arylacetonitrilase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase 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; -; 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; PTHR46044; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00920; NITRIL_CHT_1; 1.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; Hydrolase; Ligase; Reference proteome.
FT   CHAIN           1..344
FT                   /note="Arylacetonitrilase"
FT                   /id="PRO_0000451136"
FT   DOMAIN          5..290
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          324..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        167
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   344 AA;  37468 MW;  10A5C7CAA9DB1611 CRC64;
     MAPSLRVAVT QAEPEWLDLA GTVKKTCELI TEAANNGARL IAFPECWVTG YPGWIWARPV
     DFELNTKYIY NSLSIGSPEF EQIASTAKRH SIAVVLGFSE RTSTHSLYIS QAIISPQGAT
     LLHRRKIKPT HVERAVFGDG SGADLSNVVD VDFGGDVGVV KVGALACWEH TQPLLKYHTY
     SQGEVIHVAA WPPIDPHPGV EHPGLWSMSA EGCQNLSQTY AVEGGGYVLH CTGVCTEKGM
     ETMGTHKGLL FHTPGGGHSC VIGPDGRRLT QPLHGGDPAK EGIVYADLDL TNVVANRSFL
     DNVGHYSRPD LLWLGVDRKQ KQHVIPRDEE EPSRKANVVV PKQE