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Nitrilase (EC 3.5.5.1) (Arylacetonitrilase) (Indole-3-acetonitrile hydrolase) (IAN hydrolase) (Indole-3-acetonitrilase)

 NITR_PSEU2              Reviewed;         336 AA.
Q500U1;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
25-APR-2018, entry version 63.
RecName: Full=Nitrilase;
EC=3.5.5.1;
AltName: Full=Arylacetonitrilase;
AltName: Full=Indole-3-acetonitrile hydrolase;
Short=IAN hydrolase;
Short=Indole-3-acetonitrilase;
OrderedLocusNames=Psyr_0007;
Pseudomonas syringae pv. syringae (strain B728a).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
NCBI_TaxID=205918;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=B728a;
PubMed=16043691; DOI=10.1073/pnas.0504930102;
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
Kyrpides N.C., Ivanova N., Lindow S.E.;
"Comparison of the complete genome sequences of Pseudomonas syringae
pv. syringae B728a and pv. tomato DC3000.";
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
STRAIN=B728a;
PubMed=19849791; DOI=10.1111/j.1364-3703.2009.00595.x;
Howden A.J., Rico A., Mentlak T., Miguet L., Preston G.M.;
"Pseudomonas syringae pv. syringae B728a hydrolyses indole-3-
acetonitrile to the plant hormone indole-3-acetic acid.";
Mol. Plant Pathol. 10:857-865(2009).
-!- FUNCTION: Arylacetonitrilase which is capable of hydrolyzing
indole-3-acetonitrile (IAN) to the plant hormone indole-3-acetate
(IAA), and allows the plant pathogenic bacterium to use IAN as a
sole nitrogen source. Is also able to hydrolyze
phenylpropionitrile (PPN), allowing the use of this compound as a
sole nitrogen source. This enzyme may represent an additional
mechanism for IAA biosynthesis or may be used to degrade and
assimilate aldoximes and nitriles produced during host plant
secondary metabolism. {ECO:0000269|PubMed:19849791}.
-!- CATALYTIC ACTIVITY: A nitrile + 2 H(2)O = a carboxylate + NH(3).
{ECO:0000255|PROSITE-ProRule:PRU10105,
ECO:0000269|PubMed:19849791}.
-!- CATALYTIC ACTIVITY: Indole-3-acetonitrile + 2 H(2)O = indole-3-
acetate + NH(3). {ECO:0000269|PubMed:19849791}.
-!- CATALYTIC ACTIVITY: Phenylpropionitrile + 2 H(2)O =
phenylpropionate + NH(3). {ECO:0000269|PubMed:19849791}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
in medium in which the sole nitrogen source is either indole-3-
acetonitrile (IAN) or phenylpropionitrile (PPN). Their growth is
also moderately reduced in medium with ammonia as the nitrogen
source; one possible explanation for this phenotype is that the
disruption of Psyr_0007 results in the accumulation of endogenous
nitriles that can no longer be degraded and which inhibit
bacterial growth. {ECO:0000269|PubMed:19849791}.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
Nitrilase family. {ECO:0000305}.
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EMBL; CP000075; AAY35081.1; -; Genomic_DNA.
RefSeq; WP_011266126.1; NC_007005.1.
RefSeq; YP_233119.1; NC_007005.1.
ProteinModelPortal; Q500U1; -.
STRING; 205918.Psyr_0007; -.
EnsemblBacteria; AAY35081; AAY35081; Psyr_0007.
GeneID; 3365482; -.
KEGG; psb:Psyr_0007; -.
PATRIC; fig|205918.7.peg.7; -.
eggNOG; ENOG4105ES4; Bacteria.
eggNOG; COG0388; LUCA.
HOGENOM; HOG000256364; -.
KO; K01502; -.
OMA; WPSFSLY; -.
OrthoDB; POG091H0LO0; -.
BioCyc; PSYR205918:G1G4J-7-MONOMER; -.
BRENDA; 3.5.5.7; 12469.
Proteomes; UP000000426; Chromosome.
GO; GO:0000257; F:nitrilase activity; IEA:UniProtKB-EC.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
Gene3D; 3.60.110.10; -; 1.
InterPro; IPR003010; C-N_Hydrolase.
InterPro; IPR036526; C-N_Hydrolase_sf.
InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
Pfam; PF00795; CN_hydrolase; 1.
SUPFAM; SSF56317; SSF56317; 1.
PROSITE; PS50263; CN_HYDROLASE; 1.
PROSITE; PS00920; NITRIL_CHT_1; 1.
PROSITE; PS00921; NITRIL_CHT_2; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase.
CHAIN 1 336 Nitrilase.
/FTId=PRO_0000425712.
DOMAIN 5 278 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 45 45 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 127 127 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 161 161 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054, ECO:0000255|PROSITE-
ProRule:PRU10105}.
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


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