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Nitrilase 1 (EC 3.5.5.1)

 NRL1_ARATH              Reviewed;         346 AA.
P32961; O04908; Q42543; Q53YI1; Q94B53;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
20-JUN-2018, entry version 145.
RecName: Full=Nitrilase 1;
EC=3.5.5.1;
Name=NIT1; OrderedLocusNames=At3g44310; ORFNames=T10D17_100;
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], AND CHARACTERIZATION.
STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
PubMed=1555601; DOI=10.1111/j.1432-1033.1992.tb16795.x;
Bartling D., Seedorf M., Mithoefer A., Weiler E.W.;
"Cloning and expression of an Arabidopsis nitrilase which can convert
indole-3-acetonitrile to the plant hormone, indole-3-acetic acid.";
Eur. J. Biochem. 205:417-424(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Zhou L., Bartel B., Thornburg R.W.;
"Nucleotide sequence of the Arabidopsis thaliana nitrilase 1 gene.";
(er) Plant Gene Register PGR95-130(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9484465; DOI=10.1023/A:1005998918418;
Hillebrand H., Bartling D., Weiler E.W.;
"Structural analysis of the nit2/nit1/nit3 gene cluster encoding
nitrilases, enzymes catalyzing the terminal activation step in indole-
acetic acid biosynthesis in Arabidopsis thaliana.";
Plant Mol. Biol. 36:89-99(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[6]
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).
[7]
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[9]
CHARACTERIZATION.
STRAIN=cv. Landsberg erecta;
PubMed=8016109; DOI=10.1073/pnas.91.13.6021;
Bartling D., Seedorf M., Schmidt R.C., Weiler E.W.;
"Molecular characterization of two cloned nitrilases from Arabidopsis
thaliana: key enzymes in biosynthesis of the plant hormone indole-3-
acetic acid.";
Proc. Natl. Acad. Sci. U.S.A. 91:6021-6025(1994).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Can convert indole-3-acetonitrile to the plant hormone
indole-3-acetic acid.
-!- CATALYTIC ACTIVITY: A nitrile + 2 H(2)O = a carboxylate + NH(3).
{ECO:0000255|PROSITE-ProRule:PRU10105}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P32961-1; Sequence=Displayed;
Name=2;
IsoId=P32961-2; Sequence=VSP_059335;
Note=Produced by alternative initiation at Met-7 of isoform 1.
Initiator Met-1 is removed. Contains a N-acetylserine at
position 2. {ECO:0000244|PubMed:22223895};
-!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, leaves,
roots, stems, flowers and siliques. {ECO:0000269|PubMed:8022831}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development, but at a
very low level during the fruiting stage.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
Nitrilase family. {ECO:0000305}.
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EMBL; X63445; CAA45041.1; -; mRNA.
EMBL; U38845; AAB05221.1; -; Genomic_DNA.
EMBL; Y07648; CAA68935.2; -; Genomic_DNA.
EMBL; AL353865; CAB88999.1; -; Genomic_DNA.
EMBL; CP002686; AEE77887.1; -; Genomic_DNA.
EMBL; CP002686; AEE77889.1; -; Genomic_DNA.
EMBL; AY042847; AAK68787.1; -; mRNA.
EMBL; BT000040; AAN15359.1; -; mRNA.
EMBL; DQ446730; ABE65989.1; -; mRNA.
PIR; S22398; S22398.
PIR; T49147; T49147.
RefSeq; NP_001078234.1; NM_001084765.1. [P32961-1]
RefSeq; NP_851011.1; NM_180680.3. [P32961-1]
UniGene; At.23699; -.
UniGene; At.23715; -.
UniGene; At.5403; -.
UniGene; At.5404; -.
ProteinModelPortal; P32961; -.
SMR; P32961; -.
BioGrid; 8876; 3.
IntAct; P32961; 2.
MINT; P32961; -.
STRING; 3702.AT3G44310.1; -.
iPTMnet; P32961; -.
PaxDb; P32961; -.
PRIDE; P32961; -.
EnsemblPlants; AT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
EnsemblPlants; AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
GeneID; 823556; -.
Gramene; AT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
Gramene; AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
KEGG; ath:AT3G44310; -.
Araport; AT3G44310; -.
TAIR; locus:2095690; AT3G44310.
eggNOG; KOG0805; Eukaryota.
eggNOG; COG0388; LUCA.
HOGENOM; HOG000256365; -.
InParanoid; P32961; -.
KO; K01501; -.
OrthoDB; EOG09360CLO; -.
PhylomeDB; P32961; -.
BioCyc; ARA:AT3G44310-MONOMER; -.
BioCyc; MetaCyc:AT3G44310-MONOMER; -.
BRENDA; 3.5.5.1; 399.
PRO; PR:P32961; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P32961; baseline and differential.
Genevisible; P32961; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IDA:TAIR.
GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IDA:TAIR.
GO; GO:0000257; F:nitrilase activity; IDA:TAIR.
GO; GO:0009684; P:indoleacetic acid biosynthetic process; TAS: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; Alternative splicing; Complete proteome; Hydrolase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P32962}.
CHAIN 2 346 Nitrilase 1.
/FTId=PRO_0000204036.
DOMAIN 25 297 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 65 65 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 152 152 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 186 186 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054, ECO:0000255|PROSITE-
ProRule:PRU10105}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P32962}.
VAR_SEQ 1 6 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_059335.
CONFLICT 312 312 H -> Y (in Ref. 1; CAA45041).
{ECO:0000305}.
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


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