NIT_ASPOR
ID NIT_ASPOR Reviewed; 333 AA.
AC Q2U4D6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=NitAo {ECO:0000303|PubMed:23475593};
GN ORFNames=AO090020000385;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007167; BAE63579.1; -; Genomic_DNA.
DR RefSeq; XP_001824712.1; XM_001824660.1.
DR AlphaFoldDB; Q2U4D6; -.
DR SMR; Q2U4D6; -.
DR STRING; 510516.Q2U4D6; -.
DR EnsemblFungi; BAE63579; BAE63579; AO090020000385.
DR GeneID; 5996798; -.
DR KEGG; aor:AO090020000385; -.
DR VEuPathDB; FungiDB:AO090020000385; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OMA; WPSFSLY; -.
DR Proteomes; UP000006564; Chromosome 6.
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..333
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432176"
FT DOMAIN 9..284
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 333 AA; 36804 MW; 9F5C60D0CB4EB1E3 CRC64;
MTTPQPSQVR VAVTQAEPVW LDLKATVDKT CSLIAEAASK GAQLVSFPEC WIPGYPAWIW
TRPVDQELHS RYIQNSLTVS SPEMTQICKS ANENNVIVVL GFSENIHNSL YISQAIISNT
GSILTTRKKI KATHMERTIF GDAFADCLDS VVETAVGRVG ALSCWEHIQP LLKYHTCAQR
EAIHVAAWPP LFEWGGPEDE SLFSMSRDGT IALARTYAIE SSSFVLHTTA VISQEGVEKM
RTATGAIMNM PGGGSSAIFG PDGRLLSKPL LPTEEGIIYA DLEMHDIYKT KAFVDVLGHY
SRPDLLWLGV GSCDRRHVKE DAEERREDRV EVL
