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NRL3_ARATH
ID   NRL3_ARATH              Reviewed;         346 AA.
AC   P46010; O04909;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Nitrilase 3;
DE            EC=3.5.5.1;
GN   Name=NIT3; OrderedLocusNames=At3g44320; ORFNames=T10D17_110;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
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   [3]
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   [4]
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   [5]
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   [6]
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).
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   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Tightly associated with the plasma membrane.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; U09959; AAA19627.1; -; mRNA.
DR   EMBL; Y07648; CAA68936.2; -; Genomic_DNA.
DR   EMBL; AL353865; CAB89000.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77890.1; -; Genomic_DNA.
DR   EMBL; BT002773; AAO22601.1; -; mRNA.
DR   EMBL; BT004345; AAO42339.1; -; mRNA.
DR   PIR; T49148; T49148.
DR   RefSeq; NP_190018.1; NM_114300.4.
DR   AlphaFoldDB; P46010; -.
DR   SMR; P46010; -.
DR   BioGRID; 8877; 1.
DR   STRING; 3702.AT3G44320.1; -.
DR   iPTMnet; P46010; -.
DR   PaxDb; P46010; -.
DR   PRIDE; P46010; -.
DR   ProteomicsDB; 250563; -.
DR   EnsemblPlants; AT3G44320.1; AT3G44320.1; AT3G44320.
DR   GeneID; 823557; -.
DR   Gramene; AT3G44320.1; AT3G44320.1; AT3G44320.
DR   KEGG; ath:AT3G44320; -.
DR   Araport; AT3G44320; -.
DR   TAIR; locus:2095700; AT3G44320.
DR   eggNOG; KOG0805; Eukaryota.
DR   HOGENOM; CLU_030130_6_1_1; -.
DR   InParanoid; P46010; -.
DR   OMA; FPEHPDY; -.
DR   OrthoDB; 1001274at2759; -.
DR   PhylomeDB; P46010; -.
DR   BioCyc; ARA:AT3G44320-MON; -.
DR   BioCyc; MetaCyc:AT3G44320-MON; -.
DR   BRENDA; 3.5.5.1; 399.
DR   PRO; PR:P46010; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P46010; baseline and differential.
DR   Genevisible; P46010; 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:0009970; P:cellular response to sulfate starvation; IEP:TAIR.
DR   GO; GO:0051410; P:detoxification of nitrogen compound; IBA:GO_Central.
DR   GO; GO:0019762; P:glucosinolate catabolic 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..346
FT                   /note="Nitrilase 3"
FT                   /id="PRO_0000204038"
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:0007744|PubMed:22223895"
SQ   SEQUENCE   346 AA;  38022 MW;  70CFF421547F2B5E CRC64;
     MSSTEEMSSV KNTTQVIGVD PSSTVRVTIV QSSTVYNDTP ATLDKAEKFI VEAASKGAKL
     VLFPEAFIGG YPRGFRFGLA VGVHNEEGRD EFRNYHASAI KVPGPEVERL AELAGKNNVH
     LVMGAIEKDG YTLYCTALFF SPQGQFLGKH RKVMPTSLER CIWGQGDGST IPVYDTPIGK
     IGAAICWENR MPLYRTALYA KGIEIYCAPT ADYSLEWQAS MIHIAVEGGC FVLSAHQFCK
     RREFPEHPDY LFNDIVDTKE HDPTVSGGGS VIISPLGKVL AGPNYESEGL VTADLDLGDI
     ARAKLYFDVV GHYSKPDIFN LTVNEHPKKP VTFMTKVEKA EDESNK
 
 
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