ID   NRL1_ARATH              Reviewed;         346 AA.
AC   P32961; O04908; Q42543; Q53YI1; Q94B53;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=Nitrilase 1 {ECO:0000303|PubMed:8022831, ECO:0000303|Ref.3};
DE            EC=3.5.5.1 {ECO:0000255|PROSITE-ProRule:PRU10105};
GN   Name=NIT1 {ECO:0000303|PubMed:8022831, ECO:0000303|Ref.3};
GN   OrderedLocusNames=At3g44310 {ECO:0000312|Araport:AT3G44310};
GN   ORFNames=T10D17_100 {ECO:0000312|EMBL:CAB88999.1};
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 CHARACTERIZATION.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX   PubMed=1555601; DOI=10.1111/j.1432-1033.1992.tb16795.x;
RA   Bartling D., Seedorf M., Mithoefer A., Weiler E.W.;
RT   "Cloning and expression of an Arabidopsis nitrilase which can convert
RT   indole-3-acetonitrile to the plant hormone, indole-3-acetic acid.";
RL   Eur. J. Biochem. 205:417-424(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
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 the Arabidopsis thaliana nitrilase 1 gene.";
RL   (er) Plant Gene Register PGR95-130(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9484465; DOI=10.1023/a:1005998918418;
RA   Hillebrand H., Bartling D., Weiler E.W.;
RT   "Structural analysis of the nit2/nit1/nit3 gene cluster encoding
RT   nitrilases, enzymes catalyzing the terminal activation step in indole-
RT   acetic acid biosynthesis in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 36:89-99(1998).
RN   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [9]
RP   CHARACTERIZATION.
RC   STRAIN=cv. Landsberg erecta;
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   [10]
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [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   [12]
RP   INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Columbia;
RX   PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA   Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT   "A DEK domain-containing protein modulates chromatin structure and function
RT   in Arabidopsis.";
RL   Plant Cell 26:4328-4344(2014).
CC   -!- FUNCTION: Can convert indole-3-acetonitrile to the plant hormone
CC       indole-3-acetic acid.
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   -!- SUBUNIT: Interacts with DEK3. {ECO:0000269|PubMed:25387881}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P32961-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P32961-2; Sequence=VSP_059335;
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, leaves, roots,
CC       stems, flowers and siliques. {ECO:0000269|PubMed:8022831}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development, but at a very
CC       low level during the fruiting stage.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-7
CC       of isoform 1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; X63445; CAA45041.1; -; mRNA.
DR   EMBL; U38845; AAB05221.1; -; Genomic_DNA.
DR   EMBL; Y07648; CAA68935.2; -; Genomic_DNA.
DR   EMBL; AL353865; CAB88999.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77887.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77889.1; -; Genomic_DNA.
DR   EMBL; AY042847; AAK68787.1; -; mRNA.
DR   EMBL; BT000040; AAN15359.1; -; mRNA.
DR   EMBL; DQ446730; ABE65989.1; -; mRNA.
DR   PIR; S22398; S22398.
DR   PIR; T49147; T49147.
DR   RefSeq; NP_001078234.1; NM_001084765.1. [P32961-1]
DR   RefSeq; NP_851011.1; NM_180680.3. [P32961-1]
DR   AlphaFoldDB; P32961; -.
DR   EMDB; EMD-3486; -.
DR   SMR; P32961; -.
DR   BioGRID; 8876; 3.
DR   IntAct; P32961; 2.
DR   MINT; P32961; -.
DR   STRING; 3702.P32961; -.
DR   iPTMnet; P32961; -.
DR   MetOSite; P32961; -.
DR   PaxDb; 3702-AT3G44310-1; -.
DR   ProteomicsDB; 249394; -. [P32961-1]
DR   EnsemblPlants; AT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
DR   EnsemblPlants; AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
DR   GeneID; 823556; -.
DR   Gramene; AT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
DR   Gramene; AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
DR   KEGG; ath:AT3G44310; -.
DR   Araport; AT3G44310; -.
DR   TAIR; AT3G44310; NIT1.
DR   eggNOG; KOG0805; Eukaryota.
DR   InParanoid; P32961; -.
DR   OrthoDB; 644880at2759; -.
DR   PhylomeDB; P32961; -.
DR   BioCyc; ARA:AT3G44310-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G44310-MONOMER; -.
DR   BRENDA; 3.5.1.128; 399.
DR   BRENDA; 3.5.5.1; 399.
DR   PRO; PR:P32961; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P32961; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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:0000257; F:nitrilase activity; IDA:TAIR.
DR   GO; GO:0009684; P:indoleacetic acid biosynthetic process; TAS:TAIR.
DR   CDD; cd07564; nitrilases_CHs; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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; NITRILASE; 1.
DR   PANTHER; PTHR46044:SF11; NITRILASE 1-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00920; NITRIL_CHT_1; 1.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
DR   Genevisible; P32961; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32962"
FT   CHAIN           2..346
FT                   /note="Nitrilase 1"
FT                   /id="PRO_0000204036"
FT   DOMAIN          25..297
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        186
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:0000250|UniProtKB:P32962"
FT   VAR_SEQ         1..6
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059335"
FT   CONFLICT        312
FT                   /note="H -> Y (in Ref. 1; CAA45041)"
FT                   /evidence="ECO:0000305"
FT   INIT_MET        P32961-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         P32961-2:2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   346 AA;  38152 MW;  8D4F93661CAE3C1F CRC64;
     MSSTKDMSTV QNATPFNGVA PSTTVRVTIV QSSTVYNDTP ATIDKAEKYI VEAASKGAEL
     VLFPEGFIGG YPRGFRFGLA VGVHNEEGRD EFRKYHASAI HVPGPEVARL ADVARKNHVY
     LVMGAIEKEG YTLYCTVLFF SPQGQFLGKH RKLMPTSLER CIWGQGDGST IPVYDTPIGK
     LGAAICWENR MPLYRTALYA KGIELYCAPT ADGSKEWQSS MLHIAIEGGC FVLSACQFCQ
     RKHFPDHPDY LFTDWYDDKE HDSIVSQGGS VIISPLGQVL AGPNFESEGL VTADIDLGDI
     ARAKLYFDSV GHYSRPDVLH LTVNEHPRKS VTFVTKVEKA EDDSNK
//