NIT_ARTBC
ID NIT_ARTBC Reviewed; 335 AA.
AC D4B1Q8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 49.
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=NitAb {ECO:0000303|PubMed:23475593};
GN ORFNames=ARB_02388;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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=1.4 mM for phenylacetonitrile {ECO:0000269|Ref.2};
CC KM=4.0 mM for (R,S)-mandelonitrile {ECO:0000269|Ref.2};
CC Vmax=25.7 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|Ref.2};
CC Vmax=20.5 umol/min/mg enzyme toward (R,S)-mandelonitrile
CC {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 5.0-10.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 45-50 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; ABSU01000027; EFE30690.1; -; Genomic_DNA.
DR RefSeq; XP_003011330.1; XM_003011284.1.
DR AlphaFoldDB; D4B1Q8; -.
DR SMR; D4B1Q8; -.
DR STRING; 663331.D4B1Q8; -.
DR EnsemblFungi; EFE30690; EFE30690; ARB_02388.
DR GeneID; 9524231; -.
DR KEGG; abe:ARB_02388; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OMA; LHCTAVC; -.
DR Proteomes; UP000008866; 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; -; 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..335
FT /note="Arylacetonitrilase"
FT /id="PRO_0000432171"
FT DOMAIN 6..291
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 46
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 168
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 335 AA; 36085 MW; 5D37C5609D30000E CRC64;
MSGPALKVAI TQAQPKWLDL AGSVEKTVNL IAEAAKGDAR LVAFPECWIP GYPGWIWQRP
VDPIINTKYI QNSLSVNSAE MNTIKSAAKE NNIAVVLGFV EAIDTHSVYI AQAIISPKGE
LLMHRRKIKP THMERTVFGD GSGSDLTNVA DVDFGGDIGV VKVGTLACWE HALPLLKYHT
YSQKEAIHIA MWPPIDPHPG VDAPALWSMS AEGCQNLSQT HAIEGGAYVL HCTAVCNEEG
IEGMKTKGGL LFQEPGGGHS AAIAPDGRRL TKPLADGNPA AEGIVYADLD MARVVMNKGF
IDVVGHYSRP DLLWLGVDKA QKGCVVPKRE PEQDV
