NIT_NEUCR
ID NIT_NEUCR Reviewed; 327 AA.
AC V5IPE4; Q872U4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 25-MAY-2022, entry version 39.
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=NitNc {ECO:0000303|PubMed:23475593};
GN ORFNames=B23G1.100, NCU01838;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
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 [4]
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 [5]
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=2.0 mM for phenylacetonitrile {ECO:0000269|PubMed:21892598};
CC KM=3.4 mM for (R,S)-mandelonitrile {ECO:0000269|PubMed:21892598};
CC KM=1.3 mM for 2-phenylpropionitrile {ECO:0000269|PubMed:21892598};
CC Vmax=17.5 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=9.9 umol/min/mg enzyme toward (R,S)-mandelonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=0.1 umol/min/mg enzyme toward 2-phenylpropionitrile
CC {ECO:0000269|PubMed:21892598};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESA43594.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ESA43595.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX284754; CAD70472.1; -; Genomic_DNA.
DR EMBL; CM002237; ESA43594.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002237; ESA43595.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011393515.1; XM_011395213.1.
DR RefSeq; XP_011393516.1; XM_011395214.1.
DR AlphaFoldDB; V5IPE4; -.
DR SMR; V5IPE4; -.
DR STRING; 5141.EFNCRP00000001882; -.
DR EnsemblFungi; ESA43594; ESA43594; NCU01838.
DR EnsemblFungi; ESA43595; ESA43595; NCU01838.
DR GeneID; 3872769; -.
DR KEGG; ncr:NCU01838; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR BRENDA; 3.5.5.5; 3627.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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..327
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432175"
FT DOMAIN 5..289
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 327 AA; 35582 MW; CCCC80DF41406C27 CRC64;
MATTIKVAVT QAEPIWLDLQ ASIQKAVSLV HEAASNGAKI VAFSETWAPG YPGWCWARPV
DPALNTKYAY NSLTANSPEM EQLQQAAKED SIAVVIGFSE RSSSGSLYIG QAIISPQGEV
ALQRRKLKPT HMERTIFGDG SGPDLNCVAE LDFGSELGSI KVGTLNCWEH AQPLLKFHEI
QQGVVIHIAM WPPIDPYPGV EFPGLWSMTA DGCQNLSQTF AVESGAFVLH CTAVCNESGI
EAMDTRNGMV FREPGGGHSC VIGPDGRRLT QPLADKPSAE GIVYADLDLT RVVTNKSFQD
IVGHYSRPDL LWLSYDKEKK DAAVHRN
