NRL2_ARATH
ID NRL2_ARATH Reviewed; 339 AA.
AC P32962; Q96505;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Nitrilase 2;
DE EC=3.5.5.1;
GN Name=NIT2; OrderedLocusNames=At3g44300; ORFNames=T10D17_90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=8016109; DOI=10.1073/pnas.91.13.6021;
RA Bartling D., Seedorf M., Schmidt R.C., Weiler E.W.;
RT "Molecular characterization of two cloned nitrilases from Arabidopsis
RT thaliana: key enzymes in biosynthesis of the plant hormone indole-3-acetic
RT acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6021-6025(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8022831; DOI=10.1073/pnas.91.14.6649;
RA Bartel B., Fink G.R.;
RT "Differential regulation of an auxin-producing nitrilase gene family in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6649-6653(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Zhou L., Bartel B., Thornburg R.W.;
RT "Nucleotide sequence of a pathogen induced nitrilase gene from Arabidopsis
RT thaliana: Nit2.";
RL (er) Plant Gene Register PGR96-006(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP INDUCTION.
RX PubMed=22965747; DOI=10.1007/s10059-012-0122-2;
RA Huh S.U., Lee S.B., Kim H.H., Paek K.H.;
RT "ATAF2, a NAC transcription factor, binds to the promoter and regulates
RT NIT2 gene expression involved in auxin biosynthesis.";
RL Mol. Cells 34:305-313(2012).
CC -!- FUNCTION: Can convert indole-3-acetonitrile to the plant hormone
CC indole-3-acetic acid. {ECO:0000269|PubMed:8016109,
CC ECO:0000269|PubMed:8022831}.
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 -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Tightly associated with the plasma membrane.
CC -!- DEVELOPMENTAL STAGE: Barely detectable in young rosettes, but is
CC strongly expressed during bolting, flowering, and especially fruit
CC development.
CC -!- INDUCTION: By indole-3-acetonitrile, abscisic acid (ABA), salicylic
CC acid (SA), sodium nitroprusside (SNP), salt stress and dehydration
CC stress. {ECO:0000269|PubMed:22965747}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; X68305; CAA48377.1; -; mRNA.
DR EMBL; U09958; AAB60275.1; -; mRNA.
DR EMBL; U38845; AAB05220.1; -; Genomic_DNA.
DR EMBL; AL353865; CAB88998.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77886.1; -; Genomic_DNA.
DR EMBL; AY088028; AAM65574.1; -; mRNA.
DR PIR; S31969; S31969.
DR PIR; T52262; T52262.
DR RefSeq; NP_190016.1; NM_114298.3.
DR AlphaFoldDB; P32962; -.
DR SMR; P32962; -.
DR BioGRID; 8875; 1.
DR STRING; 3702.AT3G44300.1; -.
DR iPTMnet; P32962; -.
DR PaxDb; P32962; -.
DR PRIDE; P32962; -.
DR ProteomicsDB; 249395; -.
DR EnsemblPlants; AT3G44300.1; AT3G44300.1; AT3G44300.
DR GeneID; 823555; -.
DR Gramene; AT3G44300.1; AT3G44300.1; AT3G44300.
DR KEGG; ath:AT3G44300; -.
DR Araport; AT3G44300; -.
DR TAIR; locus:2095735; AT3G44300.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_1_1; -.
DR InParanoid; P32962; -.
DR OMA; KANKFIV; -.
DR OrthoDB; 1001274at2759; -.
DR PhylomeDB; P32962; -.
DR BioCyc; ARA:AT3G44300-MON; -.
DR BioCyc; MetaCyc:AT3G44300-MON; -.
DR BRENDA; 3.5.5.1; 399.
DR PRO; PR:P32962; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P32962; baseline and differential.
DR Genevisible; P32962; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IDA:TAIR.
DR GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000257; F:nitrilase activity; IDA:TAIR.
DR GO; GO:0018822; F:nitrile hydratase activity; IBA:GO_Central.
DR GO; GO:0051410; P:detoxification of nitrogen compound; IBA:GO_Central.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; TAS:TAIR.
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 Acetylation; Cell membrane; Hydrolase; Membrane; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..339
FT /note="Nitrilase 2"
FT /id="PRO_0000204037"
FT DOMAIN 18..290
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000255|PROSITE-ProRule:PRU10105"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 37
FT /note="E -> G (in Ref. 3; AAB05220)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> T (in Ref. 3; AAB05220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37153 MW; 06CDE76D2FDC24A7 CRC64;
MSTSENTPFN GVASSTIVRA TIVQASTVYN DTPATLEKAN KFIVEAASKG SELVVFPEAF
IGGYPRGFRF GLGVGVHNEE GRDEFRKYHA SAIKVPGPEV EKLAELAGKN NVYLVMGAIE
KDGYTLYCTA LFFSPQGQFL GKHRKLMPTS LERCIWGQGD GSTIPVYDTP IGKLGAAICW
ENRMPLYRTA LYAKGIELYC APTADGSKEW QSSMLHIAIE GGCFVLSACQ FCLRKDFPDH
PDYLFTDWYD DKEPDSIVSQ GGSVIISPLG QVLAGPNFES EGLITADLDL GDVARAKLYF
DSVGHYSRPD VLHLTVNEHP KKPVTFISKV EKAEDDSNK
