NIT_TALMQ
ID NIT_TALMQ Reviewed; 322 AA.
AC B6Q5I3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=NitPm {ECO:0000303|PubMed:23475593};
GN ORFNames=PMAA_032480;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000312|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
RN [2]
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 [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 4-cyanopyridine.
CC {ECO:0000269|PubMed:21892598, 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:21892598, ECO:0000269|PubMed:23475593};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.9 mM for benzonitrile {ECO:0000269|PubMed:21892598};
CC KM=11.1 mM for 3-chlorobenzonitrile {ECO:0000269|PubMed:21892598};
CC KM=2.6 mM for 4-chlorobenzonitrile {ECO:0000269|PubMed:21892598};
CC KM=11.7 mM for 2-cyanopyridine {ECO:0000269|PubMed:21892598};
CC KM=34.4 mM for 3-cyanopyridine {ECO:0000269|PubMed:21892598};
CC KM=15.4 mM for 4-cyanopyridine {ECO:0000269|PubMed:21892598};
CC KM=9.1 mM for phenylacetonitrile {ECO:0000269|PubMed:21892598};
CC Vmax=0.16 umol/min/mg enzyme toward benzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=1.9 umol/min/mg enzyme toward 3-chlorobenzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=0.13 umol/min/mg enzyme toward 4-chlorobenzonitrile
CC {ECO:0000269|PubMed:21892598};
CC Vmax=0.46 umol/min/mg enzyme toward 2-cyanopyridine
CC {ECO:0000269|PubMed:21892598};
CC Vmax=0.21 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=0.1 umol/min/mg enzyme toward phenylacetonitrile
CC {ECO:0000269|PubMed:21892598};
CC pH dependence:
CC Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:21892598};
CC Temperature dependence:
CC Optimum temperature is 30-35 degrees Celsius.
CC {ECO:0000269|PubMed:21892598};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995899; EEA28436.1; -; Genomic_DNA.
DR RefSeq; XP_002144951.1; XM_002144915.1.
DR AlphaFoldDB; B6Q5I3; -.
DR SMR; B6Q5I3; -.
DR STRING; 441960.B6Q5I3; -.
DR EnsemblFungi; EEA28436; EEA28436; PMAA_032480.
DR GeneID; 7022697; -.
DR KEGG; tmf:PMAA_032480; -.
DR VEuPathDB; FungiDB:PMAA_032480; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; B6Q5I3; -.
DR BRENDA; 3.5.5.1; 9894.
DR Proteomes; UP000001294; Unassembled WGS sequence.
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..322
FT /note="Nitrilase"
FT /id="PRO_0000432178"
FT DOMAIN 5..283
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 322 AA; 35663 MW; 14FF85AF1392E659 CRC64;
MSKIVRVGAV QSEPVWLDLE GSVDKTISLI EKAAADGVNV LGFPEVWIPG YPWSMWTSAV
INNSHIIHDY MNNSMRKDSP QMKRIQAAVK EAGMVVVLGY SERDGASLYM AQSFIDPSGE
IVHHRRKIKP THIERTIWGE GQAESLTCVI DSPFGKVGGL NCWEHLQPLL RYYEYSQGVQ
IHIASWPAEF EMPDPKKIAW LYHETGEASY RASQFFAIEG QAFVLVASQI LTEANVERNN
LTGNPVTKTP GGGFSMIFGP DGKPLCEPVD AGAEAILTAD IDLRDIDKPK AFIDVVGHYA
RPDLLSLLVN PTVDKHVTTM KK
