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 24-JAN-2024, entry version 165.
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 EMDB; EMD-3496; -.
DR SMR; P46010; -.
DR BioGRID; 8877; 1.
DR STRING; 3702.P46010; -.
DR iPTMnet; P46010; -.
DR PaxDb; 3702-AT3G44320-1; -.
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; AT3G44320; NIT3.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_1_1; -.
DR InParanoid; P46010; -.
DR OMA; FPEHPDY; -.
DR OrthoDB; 644880at2759; -.
DR PhylomeDB; P46010; -.
DR BioCyc; ARA:AT3G44320-MONOMER; -.
DR BioCyc; MetaCyc:AT3G44320-MONOMER; -.
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:0009970; P:cellular response to sulfate starvation; IEP:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic 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.
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
//
