NIT_GIBMO
ID NIT_GIBMO Reviewed; 320 AA.
AC Q19A54;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 02-JUN-2021, entry version 38.
DE RecName: Full=Nitrilase {ECO:0000303|PubMed:21892598, ECO:0000303|PubMed:23475593};
DE EC=3.5.5.1 {ECO:0000269|PubMed:21892598, ECO:0000269|PubMed:23475593};
DE AltName: Full=NitGm {ECO:0000303|PubMed:23475593};
OS Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium
OS verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=117187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC 7603;
RA Keszthelyi A., Hornok L.;
RT "Isolation and characterization of the putative nitrilase gene of Fusarium
RT verticillioides (Gibberella fujikuroi MP-A).";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 benzonitrile.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for benzonitrile {ECO:0000269|PubMed:21892598};
CC KM=0.93 mM for 3-chlorobenzonitrile {ECO:0000269|PubMed:21892598};
CC KM=1.3 mM for 4-chlorobenzonitrile {ECO:0000269|PubMed:21892598};
CC KM=3.2 mM for 3-cyanopyridine {ECO:0000269|PubMed:21892598};
CC KM=2.2 mM for 4-cyanopyridine {ECO:0000269|PubMed:21892598};
CC KM=0.75 mM for phenylacetonitrile {ECO:0000269|PubMed:21892598};
CC Vmax=9.7 umol/min/mg enzyme toward benzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=6.6 umol/min/mg enzyme toward 3-chlorobenzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=3.9 umol/min/mg enzyme toward 4-chlorobenzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=4.2 umol/min/mg enzyme toward 3-cyanopyridine
CC {ECO:0000269|PubMed:21892598};
CC Vmax=7.3 umol/min/mg enzyme toward 4-cyanopyridine
CC {ECO:0000269|PubMed:21892598};
CC Vmax=1.2 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|PubMed:21892598};
CC pH dependence:
CC Optimum pH is 7.0-10.0. {ECO:0000269|PubMed:21892598};
CC Temperature dependence:
CC Optimum temperature is 43 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; DQ534528; ABF83489.1; -; Genomic_DNA.
DR BRENDA; 3.5.5.1; 2353.
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.
FT CHAIN 1..320
FT /note="Nitrilase"
FT /id="PRO_0000432177"
FT DOMAIN 5..280
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 127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 320 AA; 36030 MW; A59094CF66225EC0 CRC64;
MSKSLKVAAI QAEPVWNDLQ GGVNKSIGLI QEAAKEGANV IGYPEVFIPG YPWSIWANSP
TENAPWINEY FKNSMEKESP EMDQIRAAVR EAGVFVVLGY SERYRGTLYI AQSFIDETGT
IVLHRRKIKP THVERAIYGD GQGESLTNVA DTKFGRVAGL NCWEHTQTLL RYYEYXQDVD
IHVSSWPSIF PQNVPEWPYH ITPECCKAFS HVVSMEGACF VLLASQIMTE ENHKKANVDG
YDYTKKSGGG FSMIFSPFGE ELVKPLAPNE EGILYADINL EEKYKAKQNL DIVGHYSRPD
QLSLRVNKHA AKPVFFANDL
