NIT1_ASPNC
ID NIT1_ASPNC Reviewed; 337 AA.
AC A2R6M7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:21892598, ECO:0000303|PubMed:23475593};
DE EC=3.5.5.1 {ECO:0000269|PubMed:21892598, ECO:0000269|PubMed:23475593};
DE EC=3.5.5.5 {ECO:0000269|PubMed:21892598, ECO:0000269|PubMed:23475593};
DE AltName: Full=NitAn {ECO:0000303|PubMed:23475593};
GN ORFNames=An16g00550;
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 {ECO:0000312|Proteomes:UP000006706};
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=20882316; DOI=10.1007/s10529-010-0421-7;
RA Kaplan O., Bezouska K., Malandra A., Vesela A.B., Petrickova A.,
RA Felsberg J., Rinagelova A., Kren V., Martinkova L.;
RT "Genome mining for the discovery of new nitrilases in filamentous fungi.";
RL Biotechnol. Lett. 33:309-312(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21892598; DOI=10.1007/s00253-011-3525-7;
RA Petrickova A., Vesela A.B., Kaplan O., Kubac D., Uhnakova B., Malandra A.,
RA Felsberg J., Rinagelova A., Weyrauch P., Kren V., Bezouska K.,
RA Martinkova L.;
RT "Purification and characterization of heterologously expressed nitrilases
RT from filamentous fungi.";
RL Appl. Microbiol. Biotechnol. 93:1553-1561(2012).
RN [4]
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 but also (R,S)-mandelonitrile, and 2-phenylpropionitrile.
CC {ECO:0000269|PubMed:20882316, ECO:0000269|PubMed:21892598,
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:20882316, ECO:0000269|PubMed:21892598,
CC 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:20882316, ECO:0000269|PubMed:21892598,
CC ECO:0000269|PubMed:23475593};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for phenylacetonitrile {ECO:0000269|PubMed:21892598};
CC KM=11.4 mM for (R,S)-mandelonitrile {ECO:0000269|PubMed:21892598};
CC KM=0.8 mM for 2-phenylpropionitrile {ECO:0000269|PubMed:21892598};
CC Vmax=10.6 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=12.4 umol/min/mg enzyme toward (R,S)-mandelonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=0.35 umol/min/mg enzyme toward 2-phenylpropionitrile
CC {ECO:0000269|PubMed:21892598};
CC pH dependence:
CC Optimum pH is 7.0-9.5. {ECO:0000269|PubMed:21892598};
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius.
CC {ECO:0000269|PubMed:21892598};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; AM270354; CAK46742.1; -; Genomic_DNA.
DR RefSeq; XP_001397369.1; XM_001397332.1.
DR AlphaFoldDB; A2R6M7; -.
DR SMR; A2R6M7; -.
DR PaxDb; A2R6M7; -.
DR EnsemblFungi; CAK46742; CAK46742; An16g00550.
DR GeneID; 4988449; -.
DR KEGG; ang:ANI_1_1358144; -.
DR VEuPathDB; FungiDB:An16g00550; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR BRENDA; 3.5.5.5; 518.
DR Proteomes; UP000006706; Chromosome 5R.
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..337
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432173"
FT DOMAIN 7..278
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 311..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 337 AA; 36949 MW; 57026C4718547C77 CRC64;
MTASTKVRVA VTQHEPVWLD LHATVDKTCR LIAEAAGNGA QLITFPECWL PGYPAWIWCR
PVDMGLFTTY LKNSLSYDSE HMRRICNAAA QHKITVVLGL SERDGNSLYI GQCTIDSTGK
IVMRRRKMKP THMERTVFGE SSGRSLLNVV DLPIGKVGAL ACWEHIQPLL KYHTMIQGEE
IHVSAWPVLH PHMGGESLWG MSQEGGTGAS QVYALESASF VLLTTAVLGP TCVKKMNLSP
PWDTLGGGAS AVIAPDGRRL TEPLPANEEG FVYADLDLDM ILTCRHFVDA CGHYSRPDLL
WLGVDTREKT QHRPEGQADN AAYGLDVPSG LVEEEGA
