NIT2_ASPNC
ID NIT2_ASPNC Reviewed; 328 AA.
AC A2RA31;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:23475593};
DE EC=3.5.5.1 {ECO:0000269|PubMed:23475593};
DE EC=3.5.5.5 {ECO:0000269|PubMed:23475593};
DE AltName: Full=NitAn2 {ECO:0000303|PubMed:23475593};
GN ORFNames=An18g01740;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23475593; DOI=10.1007/s12033-013-9656-6;
RA Kaplan O., Vesela A.B., Petrickova A., Pasquarelli F., Picmanova M.,
RA Rinagelova A., Bhalla T.C., Patek M., Martinkova L.;
RT "A comparative study of nitrilases identified by genome mining.";
RL Mol. Biotechnol. 54:996-1003(2013).
CC -!- FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile,
CC (R,S)-mandelonitrile, and 3-indolylacetonitrile.
CC {ECO:0000269|PubMed:23475593}.
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:23475593};
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:23475593};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; AM270398; CAK47246.1; -; Genomic_DNA.
DR RefSeq; XP_001398633.1; XM_001398596.2.
DR AlphaFoldDB; A2RA31; -.
DR SMR; A2RA31; -.
DR PaxDb; A2RA31; -.
DR EnsemblFungi; CAK47246; CAK47246; An18g01740.
DR GeneID; 4989734; -.
DR KEGG; ang:ANI_1_214164; -.
DR VEuPathDB; FungiDB:An18g01740; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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; Reference proteome.
FT CHAIN 1..328
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432174"
FT DOMAIN 5..278
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 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 328 AA; 35923 MW; A735AD311A29F7FE CRC64;
MLSQVRVAVT QAEPVWLDLE ATVKKTCDLI AEAAANGAQL VTFPECWIPG YPAWIWARPV
DMRLSSIYIQ NSLKIDSPQM ASIQQCAAEN KIVVVLGFSE NLHNSLYISQ AIIASDGKIL
TTRKKIKPTH MERTIFGDSF GDCLQSVVDT SAGRVGALSC WEHIQPLLKY HTYAQREQIH
VAAWPPLFPH SEDGSLFSMS TEGTSSIART YAIESQSFVL HTTTVIGQSG IDRMATSTGA
LMSTPGGGCS AIFGPDGRQL SQPIPSAEEG IIYADLDFEH IYHSKAFVDV CGHYSRPDLL
WLGVEGGVKR HVRDNATTAT PQVEQQEE
