NIT_PICGU
ID NIT_PICGU Reviewed; 317 AA.
AC A5DNJ4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Nitrilase {ECO:0000303|PubMed:23475593};
DE EC=3.5.5.1 {ECO:0000269|PubMed:23475593};
DE AltName: Full=NitMg {ECO:0000303|PubMed:23475593};
GN ORFNames=PGUG_04845;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
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. Is
CC also able to hydrolyze some aliphatic nitriles, such as
CC phenylacetonitrile. {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:23475593};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; CH408160; EDK40747.2; -; Genomic_DNA.
DR RefSeq; XP_001482890.1; XM_001482840.1.
DR AlphaFoldDB; A5DNJ4; -.
DR SMR; A5DNJ4; -.
DR STRING; 4929.XP_001482890.1; -.
DR EnsemblFungi; EDK40747; EDK40747; PGUG_04845.
DR GeneID; 5124984; -.
DR KEGG; pgu:PGUG_04845; -.
DR VEuPathDB; FungiDB:PGUG_04845; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; A5DNJ4; -.
DR OMA; GYPCWIW; -.
DR OrthoDB; 996578at2759; -.
DR Proteomes; UP000001997; 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.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..317
FT /note="Nitrilase"
FT /id="PRO_0000432179"
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 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 317 AA; 35697 MW; 8B6CDFADDEBEE78B CRC64;
MGAKVKVAVV QAEPVWFNLQ ETVKRVNELI ESAYNKGAEL IAFPEVFVPG YPTWIWTNAA
DLDRNLMYTK NSLTYDSPEF ISIIETVKKY PIHVVLGFSE KDQGSLYISQ CIIDNTGEIV
LKRRKFKPTH VERVIWGDTA DSNMKSVVTL NFKEAGPVEV GCLSCWEHMQ PLLYYNSAAQ
HEKIHIGSWP ALNDKDLGVY CFTKAGFHGL ARAYANQVQS FYLFTSILGQ RIQEALPDVK
LSPYFEKGAG CGAVFAPDGS QITEDHPDDF DGVIISELDM DKILLQKNLV DIVGHYARPD
MVSLSHNRPN TEFVNRK
