ID   NIT_TRAVS               Reviewed;         320 AA.
AC   P9WEU6;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:31795104};
DE            EC=3.5.5.1 {ECO:0000269|PubMed:31795104};
DE   AltName: Full=NitTv1 {ECO:0000303|PubMed:31795104};
GN   Name=nit; ORFNames=TRAVEDRAFT_139011;
OS   Trametes versicolor (strain FP-101664) (White-rot fungus) (Coriolus
OS   versicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=717944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP-101664;
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31795104; DOI=10.3390/ijms20235990;
RA   Rucka L., Chmatal M., Kulik N., Petraskova L., Pelantova H., Novotny P.,
RA   Prihodova R., Patek M., Martinkova L.;
RT   "Genetic and functional diversity of nitrilases in Agaricomycotina.";
RL   Int. J. Mol. Sci. 20:0-0(2019).
CC   -!- FUNCTION: Nitrilase that hydrolyzes preferentially fumaronitrile, while
CC       3-phenylpropionitrile, beta-cyano-L-alanine and 4-cyanopyridine are
CC       transformed at much lower rates. {ECO:0000269|PubMed:31795104}.
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:31795104};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; JH711783; EIW64330.1; -; Genomic_DNA.
DR   RefSeq; XP_008032838.1; XM_008034647.1.
DR   AlphaFoldDB; P9WEU6; -.
DR   SMR; P9WEU6; -.
DR   GeneID; 19409089; -.
DR   KEGG; tvs:TRAVEDRAFT_139011; -.
DR   OMA; IYADVDF; -.
DR   Proteomes; UP000054317; Unassembled WGS sequence.
DR   GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
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; 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.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="Arylacetonitrilase"
FT                   /id="PRO_0000451139"
FT   DOMAIN          5..286
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   320 AA;  34911 MW;  CACC4932ED2228FE CRC64;
     MANTIKASVV QASTAAYSLP DTLDKLEKLT RLAKERDGAQ LAVFPEAFIG GYPKMSTFGL
     VVGDRQPEGR DEFVRYAKAA IEIPSPAITR IEQISRETNV FIVVGVIERD AGTLYCTAVF
     VDPEKGYVDK HRKLVPTAME RVIWGQGDGS TLPVLDKSFE SASAPGSTVN TKLSATICWE
     NYMPLLRTYY YSQGTQIYCA PTVDARPAWQ HTMTHIALEG RCFVLSACQF AQEKDYPPDH
     AVANASARDP NNVMIAGGSV IISPLGKVLA GPLLDAEGVI SAELDLDDVL RGKFDLDVTG
     HYARNDVFEF KLREPPATSS