ILR1_ARATH
ID ILR1_ARATH Reviewed; 442 AA.
AC P54968; Q9M8S9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=IAA-amino acid hydrolase ILR1 {ECO:0000303|PubMed:7792599};
DE EC=3.5.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ILR1 {ECO:0000303|PubMed:7792599};
GN OrderedLocusNames=At3g02875 {ECO:0000312|Araport:AT3G02875};
GN ORFNames=F13E7.18 {ECO:0000312|EMBL:AAF26972.1};
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 [GENOMIC DNA], MUTAGENESIS OF GLU-69; GLY-139 AND
RP GLY-415, FUNCTION, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC STRAIN=cv. Wassilewskija;
RX PubMed=7792599; DOI=10.1126/science.7792599;
RA Bartel B., Fink G.R.;
RT "ILR1, an amidohydrolase that releases active indole-3-acetic acid from
RT conjugates.";
RL Science 268:1745-1748(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10072397; DOI=10.2307/3870866;
RA Davies R.T., Goetz D.H., Lasswell J.E., Anderson M.N., Bartel B.;
RT "IAR3 encodes an auxin conjugate hydrolase from Arabidopsis.";
RL Plant Cell 11:365-376(1999).
RN [6]
RP GENE FAMILY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=11923288; DOI=10.1074/jbc.m111955200;
RA LeClere S., Tellez R., Rampey R.A., Matsuda S.P.T., Bartel B.;
RT "Characterization of a family of IAA-amino acid conjugate hydrolases from
RT Arabidopsis.";
RL J. Biol. Chem. 277:20446-20452(2002).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15155875; DOI=10.1104/pp.104.039677;
RA Rampey R.A., LeClere S., Kowalczyk M., Ljung K., Sandberg G., Bartel B.;
RT "A family of auxin-conjugate hydrolases that contributes to free indole-3-
RT acetic acid levels during Arabidopsis germination.";
RL Plant Physiol. 135:978-988(2004).
CC -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth
CC regulator indole-3-acetic acid (IAA), including IAA-Phe, IAA-Leu and
CC IAA-Tyr (PubMed:7792599, PubMed:10072397, PubMed:11923288). Can also
CC use IAA-Ala, IAA-Gly, IAA-Met and IAA-Glu as substrates with low
CC efficiency (PubMed:7792599, PubMed:10072397, PubMed:11923288). No
CC activity with IAA-Ile, IAA-1-O-beta-D-glucose or IAA-myo-inositol
CC (PubMed:7792599, PubMed:10072397, PubMed:11923288). Is the most
CC efficient enzyme of the ILL family for IAA-Leu hydrolysis
CC (PubMed:11923288). Important for IAA-Leu and IAA-Phe hydrolysis in
CC roots (PubMed:15155875). May act with ILL2 to provide free IAA to
CC germinating seedlings (PubMed:15155875). {ECO:0000269|PubMed:10072397,
CC ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:7792599}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:7792599};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:7792599};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:7792599};
CC Note=Manganese and/or Cobalt or Copper. The ion enhances activity.
CC {ECO:0000269|PubMed:7792599};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for IAA-Ala {ECO:0000269|PubMed:11923288};
CC KM=15 uM for IAA-Leu {ECO:0000269|PubMed:11923288};
CC Vmax=14 nmol/min/mg enzyme with IAA-Ala as substrate
CC {ECO:0000269|PubMed:11923288};
CC Vmax=58 nmol/min/mg enzyme with IAA-Leu as substrate
CC {ECO:0000269|PubMed:11923288};
CC Note=kcat is 0.017 sec(-1) with IAA-Ala as substrate. kcat is 0.070
CC sec(-1) with IAA-Leu as substrate. {ECO:0000269|PubMed:11923288};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11923288};
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, siliques, seeds and
CC flowers. Detected in central regions of cotyledons, hypocotyl, radicle
CC of mature embryos and seedlings, micropyle of siliques and in pollen.
CC {ECO:0000269|PubMed:15155875}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; U23794; AAB60293.1; -; Genomic_DNA.
DR EMBL; AC018363; AAF26972.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73872.1; -; Genomic_DNA.
DR EMBL; AY054640; AAK96831.1; -; mRNA.
DR EMBL; AY081499; AAM10061.1; -; mRNA.
DR RefSeq; NP_186937.1; NM_111156.3.
DR AlphaFoldDB; P54968; -.
DR SMR; P54968; -.
DR STRING; 3702.AT3G02875.1; -.
DR MEROPS; M20.A02; -.
DR PaxDb; P54968; -.
DR PRIDE; P54968; -.
DR ProteomicsDB; 228877; -.
DR EnsemblPlants; AT3G02875.1; AT3G02875.1; AT3G02875.
DR GeneID; 821199; -.
DR Gramene; AT3G02875.1; AT3G02875.1; AT3G02875.
DR KEGG; ath:AT3G02875; -.
DR Araport; AT3G02875; -.
DR TAIR; locus:2075382; AT3G02875.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; P54968; -.
DR OMA; YLFGEDF; -.
DR OrthoDB; 1022341at2759; -.
DR PhylomeDB; P54968; -.
DR PRO; PR:P54968; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P54968; baseline and differential.
DR Genevisible; P54968; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IBA:GO_Central.
DR GO; GO:0010211; F:IAA-Leu conjugate hydrolase activity; IDA:TAIR.
DR GO; GO:0010210; F:IAA-Phe conjugate hydrolase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; IMP:TAIR.
DR CDD; cd08017; M20_IAA_Hyd; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR044757; ILR1-like_Hyd.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 1: Evidence at protein level;
KW Cobalt; Hydrolase; Manganese; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..442
FT /note="IAA-amino acid hydrolase ILR1"
FT /id="PRO_0000045468"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 140
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 401
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT MUTAGEN 69
FT /note="E->K: In ilr1-3."
FT /evidence="ECO:0000269|PubMed:7792599"
FT MUTAGEN 139
FT /note="G->D: In ilr1-1."
FT /evidence="ECO:0000269|PubMed:7792599"
FT MUTAGEN 415
FT /note="G->E: In ilr1-2."
FT /evidence="ECO:0000269|PubMed:7792599"
FT CONFLICT 6
FT /note="S -> R (in Ref. 1; AAB60293)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="H -> Y (in Ref. 1; AAB60293)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="V -> I (in Ref. 1; AAB60293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48015 MW; EA3EC8A0C6AFB931 CRC64;
MDFSGSFFVI FVTFFFLPPL SSAGSYDSGS GLESLARGML HSAKDPEFFE WMRGIRRKIH
ENPETGFQEF KTSQLVRDEL DSLGVKYKYP VAKTGVVAWI GSCSKPVFGL RADMDALPLQ
ELVEWESKSK VDGKMHACGH DTHVAMLLGA AKLLQTTKHL IKGTVKLVFQ PGEEGYAGAY
EMLKDEILDD LDGILSVHVF PSIPSGGIGS RPGTVLAGAG LFTVTVHGQG SHAATPHFSK
DPVLAASSAV VALQQIVSRE LDPLEAGVVT VGYIEGGHAQ NVIPQSAKFG GTFRSLSNDG
LLFIQRRIKE ISEAQASVYR CKAEVNFEEK KPSLHPVMNN DEGLYEHGKK VAEAMIGKNN
FHDFPVTMGG EDFSFFTQKT KAAIFVLGVK NETLGAGKPL HSPYFFVDEE ALPVGAALHA
AMAVSYLDEH GHSHEEEVKS EL
