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Protein

Nitrilase 1

Gene

NIT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can convert indole-3-acetonitrile to the plant hormone indole-3-acetic acid.

Catalytic activityi

A nitrile + 2 H2O = a carboxylate + NH3.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Proton acceptorPROSITE-ProRule annotation
Active sitei152 – 1521Proton donorPROSITE-ProRule annotation
Active sitei186 – 1861NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. indole-3-acetonitrile nitrilase activity Source: TAIR
  2. indole-3-acetonitrile nitrile hydratase activity Source: TAIR
  3. nitrilase activity Source: TAIR

GO - Biological processi

  1. indoleacetic acid biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciARA:AT3G44310-MONOMER.
ARA:GQT-941-MONOMER.
ARA:GQT-942-MONOMER.
MetaCyc:AT3G44310-MONOMER.
BRENDAi3.5.5.1. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrilase 1 (EC:3.5.5.1)
Gene namesi
Name:NIT1
Ordered Locus Names:At3g44310
ORF Names:T10D17_100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G44310.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. cytosol Source: TAIR
  4. plasma membrane Source: TAIR
  5. plasmodesma Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 346345Nitrilase 1PRO_0000204036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

PaxDbiP32961.
PRIDEiP32961.

Expressioni

Tissue specificityi

Expressed in cotyledons, hypocotyls, leaves, roots, stems, flowers and siliques.1 Publication

Developmental stagei

Expressed throughout development, but at a very low level during the fruiting stage.

Gene expression databases

ExpressionAtlasiP32961. baseline and differential.
GenevestigatoriP32961.

Interactioni

Protein-protein interaction databases

BioGridi8876. 2 interactions.
IntActiP32961. 2 interactions.
STRINGi3702.AT3G44310.3-P.

Structurei

3D structure databases

ProteinModelPortaliP32961.
SMRiP32961. Positions 25-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 320296CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0388.
HOGENOMiHOG000256365.
InParanoidiP32961.
KOiK01501.
OMAiYHANAID.
PhylomeDBiP32961.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR000132. Nitrilase/CN_hydratase_CS.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
PS00920. NITRIL_CHT_1. 1 hit.
PS00921. NITRIL_CHT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P32961-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSTKDMSTV QNATPFNGVA PSTTVRVTIV QSSTVYNDTP ATIDKAEKYI
60 70 80 90 100
VEAASKGAEL VLFPEGFIGG YPRGFRFGLA VGVHNEEGRD EFRKYHASAI
110 120 130 140 150
HVPGPEVARL ADVARKNHVY LVMGAIEKEG YTLYCTVLFF SPQGQFLGKH
160 170 180 190 200
RKLMPTSLER CIWGQGDGST IPVYDTPIGK LGAAICWENR MPLYRTALYA
210 220 230 240 250
KGIELYCAPT ADGSKEWQSS MLHIAIEGGC FVLSACQFCQ RKHFPDHPDY
260 270 280 290 300
LFTDWYDDKE HDSIVSQGGS VIISPLGQVL AGPNFESEGL VTADIDLGDI
310 320 330 340
ARAKLYFDSV GHYSRPDVLH LTVNEHPRKS VTFVTKVEKA EDDSNK
Length:346
Mass (Da):38,152
Last modified:February 5, 2008 - v2
Checksum:i8D4F93661CAE3C1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121H → Y in CAA45041 (PubMed:1555601).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63445 mRNA. Translation: CAA45041.1.
U38845 Genomic DNA. Translation: AAB05221.1.
Y07648 Genomic DNA. Translation: CAA68935.2.
AL353865 Genomic DNA. Translation: CAB88999.1.
CP002686 Genomic DNA. Translation: AEE77887.1.
CP002686 Genomic DNA. Translation: AEE77889.1.
AY042847 mRNA. Translation: AAK68787.1.
BT000040 mRNA. Translation: AAN15359.1.
DQ446730 mRNA. Translation: ABE65989.1.
PIRiS22398.
T49147.
RefSeqiNP_001078234.1. NM_001084765.1. [P32961-1]
NP_851011.1. NM_180680.2. [P32961-1]
UniGeneiAt.23699.
At.23715.
At.5403.
At.5404.

Genome annotation databases

EnsemblPlantsiAT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
GeneIDi823556.
KEGGiath:AT3G44310.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63445 mRNA. Translation: CAA45041.1.
U38845 Genomic DNA. Translation: AAB05221.1.
Y07648 Genomic DNA. Translation: CAA68935.2.
AL353865 Genomic DNA. Translation: CAB88999.1.
CP002686 Genomic DNA. Translation: AEE77887.1.
CP002686 Genomic DNA. Translation: AEE77889.1.
AY042847 mRNA. Translation: AAK68787.1.
BT000040 mRNA. Translation: AAN15359.1.
DQ446730 mRNA. Translation: ABE65989.1.
PIRiS22398.
T49147.
RefSeqiNP_001078234.1. NM_001084765.1. [P32961-1]
NP_851011.1. NM_180680.2. [P32961-1]
UniGeneiAt.23699.
At.23715.
At.5403.
At.5404.

3D structure databases

ProteinModelPortaliP32961.
SMRiP32961. Positions 25-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8876. 2 interactions.
IntActiP32961. 2 interactions.
STRINGi3702.AT3G44310.3-P.

Proteomic databases

PaxDbiP32961.
PRIDEiP32961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G44310.1; AT3G44310.1; AT3G44310. [P32961-1]
AT3G44310.3; AT3G44310.3; AT3G44310. [P32961-1]
GeneIDi823556.
KEGGiath:AT3G44310.

Organism-specific databases

TAIRiAT3G44310.

Phylogenomic databases

eggNOGiCOG0388.
HOGENOMiHOG000256365.
InParanoidiP32961.
KOiK01501.
OMAiYHANAID.
PhylomeDBiP32961.

Enzyme and pathway databases

BioCyciARA:AT3G44310-MONOMER.
ARA:GQT-941-MONOMER.
ARA:GQT-942-MONOMER.
MetaCyc:AT3G44310-MONOMER.
BRENDAi3.5.5.1. 399.

Gene expression databases

ExpressionAtlasiP32961. baseline and differential.
GenevestigatoriP32961.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR000132. Nitrilase/CN_hydratase_CS.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
PS00920. NITRIL_CHT_1. 1 hit.
PS00921. NITRIL_CHT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of an Arabidopsis nitrilase which can convert indole-3-acetonitrile to the plant hormone, indole-3-acetic acid."
    Bartling D., Seedorf M., Mithoefer A., Weiler E.W.
    Eur. J. Biochem. 205:417-424(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: cv. Landsberg erecta.
    Tissue: Leaf.
  2. "Differential regulation of an auxin-producing nitrilase gene family in Arabidopsis thaliana."
    Bartel B., Fink G.R.
    Proc. Natl. Acad. Sci. U.S.A. 91:6649-6653(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "Nucleotide sequence of the Arabidopsis thaliana nitrilase 1 gene."
    Zhou L., Bartel B., Thornburg R.W.
    Plant Gene Register PGR95-130
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  4. "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."
    Hillebrand H., Bartling D., Weiler E.W.
    Plant Mol. Biol. 36:89-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    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.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  9. "Molecular characterization of two cloned nitrilases from Arabidopsis thaliana: key enzymes in biosynthesis of the plant hormone indole-3-acetic acid."
    Bartling D., Seedorf M., Schmidt R.C., Weiler E.W.
    Proc. Natl. Acad. Sci. U.S.A. 91:6021-6025(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: cv. Landsberg erecta.
  10. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNRL1_ARATH
AccessioniPrimary (citable) accession number: P32961
Secondary accession number(s): O04908
, Q42543, Q53YI1, Q94B53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 5, 2008
Last modified: March 4, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.