NITR_PSEU2
ID NITR_PSEU2 Reviewed; 336 AA.
AC Q500U1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Nitrilase;
DE EC=3.5.5.1;
DE AltName: Full=Arylacetonitrilase;
DE AltName: Full=Indole-3-acetonitrile hydrolase;
DE Short=IAN hydrolase;
DE Short=Indole-3-acetonitrilase;
GN OrderedLocusNames=Psyr_0007;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=B728a;
RX PubMed=19849791; DOI=10.1111/j.1364-3703.2009.00595.x;
RA Howden A.J., Rico A., Mentlak T., Miguet L., Preston G.M.;
RT "Pseudomonas syringae pv. syringae B728a hydrolyses indole-3-acetonitrile
RT to the plant hormone indole-3-acetic acid.";
RL Mol. Plant Pathol. 10:857-865(2009).
CC -!- FUNCTION: Arylacetonitrilase which is capable of hydrolyzing indole-3-
CC acetonitrile (IAN) to the plant hormone indole-3-acetate (IAA), and
CC allows the plant pathogenic bacterium to use IAN as a sole nitrogen
CC source. Is also able to hydrolyze phenylpropionitrile (PPN), allowing
CC the use of this compound as a sole nitrogen source. This enzyme may
CC represent an additional mechanism for IAA biosynthesis or may be used
CC to degrade and assimilate aldoximes and nitriles produced during host
CC plant secondary metabolism. {ECO:0000269|PubMed:19849791}.
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:0000255|PROSITE-ProRule:PRU10105,
CC ECO:0000269|PubMed:19849791};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)acetonitrile + 2 H2O = (indol-3-yl)acetate +
CC NH4(+); Xref=Rhea:RHEA:45776, ChEBI:CHEBI:15377, ChEBI:CHEBI:17566,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30854; EC=3.5.5.1;
CC Evidence={ECO:0000269|PubMed:19849791};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + phenylpropanonitrile = 3-phenylpropanoate + NH4(+);
CC Xref=Rhea:RHEA:45784, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:51057, ChEBI:CHEBI:85426; EC=3.5.5.1;
CC Evidence={ECO:0000269|PubMed:19849791};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in
CC medium in which the sole nitrogen source is either indole-3-
CC acetonitrile (IAN) or phenylpropionitrile (PPN). Their growth is also
CC moderately reduced in medium with ammonia as the nitrogen source; one
CC possible explanation for this phenotype is that the disruption of
CC Psyr_0007 results in the accumulation of endogenous nitriles that can
CC no longer be degraded and which inhibit bacterial growth.
CC {ECO:0000269|PubMed:19849791}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; CP000075; AAY35081.1; -; Genomic_DNA.
DR RefSeq; WP_011266126.1; NC_007005.1.
DR RefSeq; YP_233119.1; NC_007005.1.
DR AlphaFoldDB; Q500U1; -.
DR SMR; Q500U1; -.
DR STRING; 205918.Psyr_0007; -.
DR EnsemblBacteria; AAY35081; AAY35081; Psyr_0007.
DR KEGG; psb:Psyr_0007; -.
DR PATRIC; fig|205918.7.peg.7; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_030130_6_0_6; -.
DR OMA; WPSFSLY; -.
DR BRENDA; 3.5.5.7; 12469.
DR Proteomes; UP000000426; Chromosome.
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; 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.
FT CHAIN 1..336
FT /note="Nitrilase"
FT /id="PRO_0000425712"
FT DOMAIN 5..278
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 /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000255|PROSITE-ProRule:PRU10105"
SQ SEQUENCE 336 AA; 36553 MW; EC3DF2A762E37729 CRC64;
MKEPLKVACV QAAPVFLDLD ATVDKTITLM EQAAAAGAGL IAFPETWIPG YPWFLWLDAP
AWNMPLVQRY HQQSLVLDSV QARRISDAAR HLGLYVVLGY SERNKASLYI GQWIIDDHGE
TVGVRRKLKA THVERTMFGE GDGASLRTFE TPVGVLGALC CWEHLQPLSK YAMYAQNEQI
HVAAWPSFSL YRNATSALGP EVNTAASRVY AAEGQCFVLA PCAIVSPEMI EMLCDSDAKR
SLLQAGGGHA RIFGPDGSDL ATPLGEHEEG LLYATLDPAA LTLAKVAADP AGHYSRPDVT
RLMFNPNPTP CVVDLPDLPI SSESIELLRP DIALEV
