NIT_HYPVG
ID NIT_HYPVG Reviewed; 329 AA.
AC G9N4E3; A0A0P1DJB0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:26521240};
DE EC=3.5.5.1 {ECO:0000250|UniProtKB:C7YS90};
DE EC=3.5.5.5 {ECO:0000250|UniProtKB:C7YS90};
DE AltName: Full=NitTv {ECO:0000303|PubMed:26521240};
GN ORFNames=TRIVIDRAFT_77162;
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071;
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=Gv29-8 / FGSC 10586;
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile
CC and heteroaromatic nitriles, but has significantly lower activity for
CC (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:0000250|UniProtKB:C7YS90};
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:0000250|UniProtKB:C7YS90};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; LN875498; CTQ87322.1; -; Genomic_DNA.
DR EMBL; ABDF02000086; EHK18468.1; -; Genomic_DNA.
DR RefSeq; XP_013952666.1; XM_014097191.1.
DR AlphaFoldDB; G9N4E3; -.
DR SMR; G9N4E3; -.
DR STRING; 413071.G9N4E3; -.
DR EnsemblFungi; EHK18468; EHK18468; TRIVIDRAFT_77162.
DR GeneID; 25797893; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_77162; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; G9N4E3; -.
DR OMA; GYPCWIW; -.
DR OrthoDB; 996578at2759; -.
DR BRENDA; 3.5.5.5; 17448.
DR Proteomes; UP000007115; Unassembled WGS sequence.
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: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..329
FT /note="Arylacetonitrilase"
FT /id="PRO_0000451137"
FT DOMAIN 6..279
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 126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 329 AA; 36271 MW; DBAB4C51CEF708A4 CRC64;
MPDRVVRVAV TQAEPVWLDL QATIEKTCRL ITEAASNNAQ LVAFPETWIP GYPCWIWSRL
VDFDLNVAYI KNSLRVDSPE MERLQACARE AGIAVSLGFS ENSNNSLYIS NVLIGSDGEI
KVHRRKMKPT HMERTVFGDA SGHCLQSVAQ LPFGRVGSLS CWEHIQPLLK YNTITQNEEI
HVAAWPPLNS EVGDEIPWSM TAEGCKTLSR TYAIESGTFV LHCTAVISES GINSLGTLGG
ALMSTPGGGH STIFGPDGRR ITDHIEETSE GIVYANLDMD ELVVNKMFAD CTGHYSRPDL
LWLGVSQEIK PVVRPQRAEV DKGTNDQVE
