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Bifunctional nitrilase/nitrile hydratase NIT4 (EC 3.5.5.1) (EC 3.5.5.4) (EC 4.2.1.65) (Cyanoalanine nitrilase) (Nitrilase 4)

 NRL4_ARATH              Reviewed;         355 AA.
P46011; Q8L9L4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
05-DEC-2018, entry version 134.
RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4;
EC=3.5.5.1;
EC=3.5.5.4;
EC=4.2.1.65;
AltName: Full=Cyanoalanine nitrilase;
AltName: Full=Nitrilase 4;
Name=NIT4; OrderedLocusNames=At5g22300; ORFNames=MWD9.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=8022831; DOI=10.1073/pnas.91.14.6649;
Bartel B., Fink G.R.;
"Differential regulation of an auxin-producing nitrilase gene family
in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 91:6649-6653(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, MUTAGENESIS OF CYS-197, ACTIVITY REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11060302; DOI=10.1074/jbc.M007890200;
Piotrowski M., Schoenfelder S., Weiler E.W.;
"The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco
encode beta-cyano-L-alanine hydratase/nitrilase.";
J. Biol. Chem. 276:2616-2621(2001).
-!- FUNCTION: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low
activity with 3-phenylpropionitrile (PPN) or allylcyanide and no
activity with indole-3-acetonitrile. Not associated with auxin
production but may be involved in cyanide detoxification.
{ECO:0000269|PubMed:11060302}.
-!- CATALYTIC ACTIVITY:
Reaction=a nitrile + 2 H2O = a carboxylate + NH4(+);
Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10105};
-!- CATALYTIC ACTIVITY:
Reaction=3-cyano-L-alanine + 2 H2O = L-aspartate + NH4(+);
Xref=Rhea:RHEA:11188, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
ChEBI:CHEBI:29991, ChEBI:CHEBI:77860; EC=3.5.5.4;
-!- CATALYTIC ACTIVITY:
Reaction=L-asparagine = 3-cyano-L-alanine + H2O;
Xref=Rhea:RHEA:15385, ChEBI:CHEBI:15377, ChEBI:CHEBI:58048,
ChEBI:CHEBI:77860; EC=4.2.1.65;
-!- ACTIVITY REGULATION: Both catalytic activities are inhibited by N-
ethylmaleimide and are up-regulated during senescence.
{ECO:0000269|PubMed:11060302}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.74 mM for Ala(CN) (for the nitrilase activity)
{ECO:0000269|PubMed:11060302};
KM=0.70 mM for Ala(CN) (for the nitrile hydratase activity)
{ECO:0000269|PubMed:11060302};
Vmax=1.84 umol/sec/mg enzyme for the nitrilase activity
{ECO:0000269|PubMed:11060302};
Vmax=2.55 umol/sec/mg enzyme for the nitrile hydratase activity
{ECO:0000269|PubMed:11060302};
pH dependence:
Optimum pH is 7-9 for both activities.
{ECO:0000269|PubMed:11060302};
Temperature dependence:
Optimum temperature for both activities is 40 degrees Celsius.
{ECO:0000269|PubMed:11060302};
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
Cytoplasmic side. Note=Tightly associated with the plasma
membrane.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
Nitrilase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM65906.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U09961; AAA19628.1; -; mRNA.
EMBL; AB007651; BAB08328.1; -; Genomic_DNA.
EMBL; CP002688; AED93008.1; -; Genomic_DNA.
EMBL; AF372965; AAK50102.1; -; mRNA.
EMBL; AY124854; AAM70563.1; -; mRNA.
EMBL; AY088367; AAM65906.1; ALT_INIT; mRNA.
PIR; T52265; T52265.
RefSeq; NP_197622.1; NM_122135.6.
UniGene; At.49047; -.
ProteinModelPortal; P46011; -.
SMR; P46011; -.
STRING; 3702.AT5G22300.1; -.
PaxDb; P46011; -.
PRIDE; P46011; -.
EnsemblPlants; AT5G22300.1; AT5G22300.1; AT5G22300.
GeneID; 832290; -.
Gramene; AT5G22300.1; AT5G22300.1; AT5G22300.
KEGG; ath:AT5G22300; -.
Araport; AT5G22300; -.
TAIR; locus:2176377; AT5G22300.
eggNOG; KOG0805; Eukaryota.
eggNOG; COG0388; LUCA.
HOGENOM; HOG000256365; -.
InParanoid; P46011; -.
KO; K13035; -.
OMA; TMRHIAL; -.
OrthoDB; EOG09360CLO; -.
PhylomeDB; P46011; -.
PRO; PR:P46011; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P46011; baseline and differential.
Genevisible; P46011; AT.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047558; F:3-cyanoalanine hydratase activity; IDA:TAIR.
GO; GO:0047427; F:cyanoalanine nitrilase activity; IDA:TAIR.
GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IDA:TAIR.
GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IBA:GO_Central.
GO; GO:0000257; F:nitrilase activity; IDA:TAIR.
GO; GO:0018822; F:nitrile hydratase activity; IDA:TAIR.
GO; GO:0019500; P:cyanide catabolic process; IBA:GO_Central.
GO; GO:0019499; P:cyanide metabolic process; IEP:TAIR.
GO; GO:0051410; P:detoxification of nitrogen compound; IEP:TAIR.
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;
Acetylation; Cell membrane; Complete proteome; Hydrolase; Lyase;
Membrane; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P32962}.
CHAIN 2 355 Bifunctional nitrilase/nitrile hydratase
NIT4.
/FTId=PRO_0000204039.
DOMAIN 36 308 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 76 76 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 163 163 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 197 197 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054, ECO:0000255|PROSITE-
ProRule:PRU10105}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P32962}.
MUTAGEN 197 197 C->A: Loss of nitrilase activity and 95%
reduction of the nitrile hydratase
activity. {ECO:0000269|PubMed:11060302}.
SEQUENCE 355 AA; 38895 MW; 8A042F7DFC5600F6 CRC64;
MSMQQETSHM TAAPQTNGHQ IFPEIDMSAG DSSSIVRATV VQASTVFYDT PATLDKAERL
LSEAAENGSQ LVVFPEAFIG GYPRGSTFEL AIGSRTAKGR DDFRKYHASA IDVPGPEVER
LALMAKKYKV YLVMGVIERE GYTLYCTVLF FDSQGLFLGK HRKLMPTALE RCIWGFGDGS
TIPVFDTPIG KIGAAICWEN RMPSLRTAMY AKGIEIYCAP TADSRETWLA SMTHIALEGG
CFVLSANQFC RRKDYPSPPE YMFSGSEESL TPDSVVCAGG SSIISPLGIV LAGPNYRGEA
LITADLDLGD IARAKFDFDV VGHYSRPEVF SLNIREHPRK AVSFKTSKVM EDESV


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