NIT_AURST
ID NIT_AURST Reviewed; 331 AA.
AC A0A0P1DJE3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
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=NitAd {ECO:0000303|PubMed:26521240};
GN Name=nit; ORFNames=AURDEDRAFT_89823;
OS Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS (Auricularia delicata (strain TFB10046)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Auriculariaceae; Auricularia.
OX NCBI_TaxID=717982;
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=TFB-10046 / SS5;
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).
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; LN875494; CTQ87318.1; -; Genomic_DNA.
DR EMBL; JH687787; EJD42068.1; -; Genomic_DNA.
DR RefSeq; XP_007349843.1; XM_007349781.1.
DR AlphaFoldDB; A0A0P1DJE3; -.
DR SMR; A0A0P1DJE3; -.
DR KEGG; adl:AURDEDRAFT_89823; -.
DR OMA; LHCTAVC; -.
DR BRENDA; 3.5.5.5; 17447.
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 Hydrolase.
FT CHAIN 1..331
FT /note="Arylacetonitrilase"
FT /id="PRO_0000451133"
FT DOMAIN 5..290
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
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 331 AA; 35797 MW; D1936749F7D213AF CRC64;
MPHTLRVAVT QAEPEWLDLA GTVEKTCNLI GEAAENGARL IAFPECWVPG YPGWIWARPV
DVELNTKYIY NSLSLGSPEF ETIQAAAKRH SIAVVMGFSG RAPSDSLYIA QAIISPDGEV
LMHRRKVKPT HAERTVFGDG SGADLSNVVD VDFGGEIGTV KVGALACWEH TQPLLKYHTL
SLGAAVHVAM WPPLDPHGGV EHPGLWSMSA EGCQSLSQTY AIESGAYVLH CTAVCTEKGR
EAMRTHDGLL FHTPGGGHSC VLGPDGRRLT QALHGGDPAK EGVVYADLDL SKVVANRAFL
DNVGHYSRPD LLWLGVDRRE KGHVVDGERR L
