ID NIT_FUSV7 Reviewed; 339 AA.
AC C7YS90;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:23475593, ECO:0000303|Ref.2};
DE EC=3.5.5.1 {ECO:0000269|PubMed:23475593, ECO:0000269|Ref.2};
DE EC=3.5.5.5 {ECO:0000269|PubMed:23475593, ECO:0000269|Ref.2};
DE AltName: Full=NitNh {ECO:0000303|PubMed:23475593};
GN ORFNames=NECHADRAFT_80653;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.3109/10242422.2012.758117;
RA Vesela A.B., Petrickova A., Weyrauch P., Martinkova L.;
RT "Heterologous expression, purification and characterization of
RT arylacetonitrilases from Nectria haematococca and Arthroderma benhamiae.";
RL Biocatal. Biotransformation 31:49-56(2013).
RN [3]
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, ECO:0000269|Ref.2}.
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, ECO:0000269|Ref.2};
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, ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.3 mM for phenylacetonitrile {ECO:0000269|Ref.2};
CC KM=9.9 mM for (R,S)-mandelonitrile {ECO:0000269|Ref.2};
CC Vmax=111.1 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|Ref.2};
CC Vmax=31.3 umol/min/mg enzyme toward (R,S)-mandelonitrile
CC {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 5.5-8.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; GG698899; EEU45207.1; -; Genomic_DNA.
DR RefSeq; XP_003050920.1; XM_003050874.1.
DR AlphaFoldDB; C7YS90; -.
DR SMR; C7YS90; -.
DR STRING; 660122.C7YS90; -.
DR EnsemblFungi; NechaT80653; NechaP80653; NechaG80653.
DR GeneID; 9666163; -.
DR KEGG; nhe:NECHADRAFT_80653; -.
DR VEuPathDB; FungiDB:NECHADRAFT_80653; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; C7YS90; -.
DR OMA; GYPCWIW; -.
DR OrthoDB; 2785533at2759; -.
DR Proteomes; UP000005206; 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; Carbon-nitrogen hydrolase; 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:SF1; CN HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46044; NITRILASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00920; NITRIL_CHT_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..339
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432172"
FT DOMAIN 5..290
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 339 AA; 36773 MW; 5CE9EA7B4E06CFFD CRC64;
MACPIRVAVT QAEPVYLDLA ASVKKACGLI AEAAQNGAKL VAFSECWLPG YPAWIWARPV
DFELQTRYIY NSLPIESEAM ELVKATAKEH SIAVALGFSE QSPSHSIYIS QAIISPQGEV
VMHRRKIKPT HMERTLFGDG SGADLNNVVE VDFGAEHGKI KVGCFACWEH TQPLLKYHSI
SQGEAIHISM WPPIDPSAGV DHPGLWSMTA DGCQNLSQTY AIESTAYVLH STSVCTQKGI
ETLKTQDGLS CRQPGGGHSC VIGPDGRRLT APLGDGSPDA EGIVYADLDL TKVVATRGFL
DIVGHYSRPD LLWLGVDREQ KENIIAKQHK AAEQEAVQG
//
