SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P32961

- NRL1_ARATH

UniProt

P32961 - NRL1_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Nitrilase 1
Gene
NIT1, At3g44310, T10D17_100
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Proton acceptor By similarity
Active sitei152 – 1521Proton donor By similarity
Active sitei186 – 1861Nucleophile By similarity

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 – 11Removed By similarity
Chaini2 – 346345Nitrilase 1
PRO_0000204036Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Ubiquitinated.

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

GenevestigatoriP32961.

Interactioni

Protein-protein interaction databases

BioGridi8876. 2 interactions.
IntActiP32961. 1 interaction.
STRINGi3702.AT3G44310.3-P.

Structurei

3D structure databases

ProteinModelPortaliP32961.
SMRiP32961. Positions 25-325.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 320296CN hydrolase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0388.
HOGENOMiHOG000256365.
InParanoidiP32961.
KOiK01501.
OMAiEGREWIN.
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. Align

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

MSSTKDMSTV QNATPFNGVA PSTTVRVTIV QSSTVYNDTP ATIDKAEKYI    50
VEAASKGAEL VLFPEGFIGG YPRGFRFGLA VGVHNEEGRD EFRKYHASAI 100
HVPGPEVARL ADVARKNHVY LVMGAIEKEG YTLYCTVLFF SPQGQFLGKH 150
RKLMPTSLER CIWGQGDGST IPVYDTPIGK LGAAICWENR MPLYRTALYA 200
KGIELYCAPT ADGSKEWQSS MLHIAIEGGC FVLSACQFCQ RKHFPDHPDY 250
LFTDWYDDKE HDSIVSQGGS VIISPLGQVL AGPNFESEGL VTADIDLGDI 300
ARAKLYFDSV GHYSRPDVLH LTVNEHPRKS VTFVTKVEKA EDDSNK 346
Length:346
Mass (Da):38,152
Last modified:February 5, 2008 - v2
Checksum:i8D4F93661CAE3C1F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121H → Y in CAA45041. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S22398.
T49147.
RefSeqi NP_001078234.1. NM_001084765.1. [P32961-1 ]
NP_851011.1. NM_180680.2. [P32961-1 ]
UniGenei At.23699.
At.23715.
At.5403.
At.5404.

3D structure databases

ProteinModelPortali P32961.
SMRi P32961. Positions 25-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 8876. 2 interactions.
IntActi P32961. 1 interaction.
STRINGi 3702.AT3G44310.3-P.

Proteomic databases

PaxDbi P32961.
PRIDEi P32961.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G44310.1 ; AT3G44310.1 ; AT3G44310 . [P32961-1 ]
AT3G44310.3 ; AT3G44310.3 ; AT3G44310 . [P32961-1 ]
GeneIDi 823556.
KEGGi ath:AT3G44310.

Organism-specific databases

TAIRi AT3G44310.

Phylogenomic databases

eggNOGi COG0388.
HOGENOMi HOG000256365.
InParanoidi P32961.
KOi K01501.
OMAi EGREWIN.
PhylomeDBi P32961.

Enzyme and pathway databases

BioCyci ARA:AT3G44310-MONOMER.
ARA:GQT-941-MONOMER.
ARA:GQT-942-MONOMER.
MetaCyc:AT3G44310-MONOMER.
BRENDAi 3.5.5.1. 399.

Gene expression databases

Genevestigatori P32961.

Family and domain databases

Gene3Di 3.60.110.10. 1 hit.
InterProi IPR003010. C-N_Hydrolase.
IPR000132. Nitrilase/CN_hydratase_CS.
[Graphical view ]
Pfami PF00795. CN_hydrolase. 1 hit.
[Graphical view ]
SUPFAMi SSF56317. SSF56317. 1 hit.
PROSITEi PS50263. CN_HYDROLASE. 1 hit.
PS00920. NITRIL_CHT_1. 1 hit.
PS00921. NITRIL_CHT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 116 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