ILL2_ARATH
ID ILL2_ARATH Reviewed; 439 AA.
AC P54970; O49221;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=IAA-amino acid hydrolase ILR1-like 2 {ECO:0000303|PubMed:7792599};
DE EC=3.5.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ILL2 {ECO:0000303|PubMed:7792599};
GN OrderedLocusNames=At5g56660 {ECO:0000312|Araport:AT5G56660};
GN ORFNames=MIK19.11 {ECO:0000312|EMBL:BAB09884.1};
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
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 [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-439.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-439, AND SUBUNIT.
RX PubMed=18543330; DOI=10.1002/prot.22124;
RA Bitto E., Bingman C.A., Bittova L., Houston N.L., Boston R.S., Fox B.G.,
RA Phillips G.N. Jr.;
RT "X-ray structure of ILL2, an auxin-conjugate amidohydrolase from
RT Arabidopsis thaliana.";
RL Proteins 74:61-71(2009).
CC -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth
CC regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Leu, IAA-
CC Met, IAA-Phe, IAA-Ser, IAA-Thr, IAA-Tyr and IAA-Val (PubMed:11923288).
CC Is the most efficient enzyme of the ILL family for IAA-Ala
CC (PubMed:11923288). Not important for IAA-Leu hydrolysis in roots
CC (PubMed:15155875). May act with ILR1 to provide free IAA to germinating
CC seedlings (PubMed:15155875). {ECO:0000269|PubMed:11923288,
CC ECO:0000269|PubMed:15155875}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11923288};
CC Note=The Mn(2+) ion enhances activity. {ECO:0000269|PubMed:11923288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for IAA-Ala {ECO:0000269|PubMed:11923288};
CC KM=126 uM for IAA-Leu {ECO:0000269|PubMed:11923288};
CC Vmax=1700 nmol/min/mg enzyme with IAA-Ala as substrate
CC {ECO:0000269|PubMed:11923288};
CC Vmax=220 nmol/min/mg enzyme with IAA-Leu as substrate
CC {ECO:0000269|PubMed:11923288};
CC Note=kcat is 2.1 sec(-1) with IAA-Ala as substrate. kcat is 0.27
CC sec(-1) with IAA-Leu as substrate. {ECO:0000269|PubMed:11923288};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:11923288};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18543330}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, siliques, seeds and
CC flowers. Detected in the distal tips of cotyledons and seedling leaves,
CC hydathodes of leaves from mature plants, pollen, ovules and developing
CC seeds. {ECO:0000269|PubMed:15155875}.
CC -!- DISRUPTION PHENOTYPE: No effect on the sensitivity to the inhibition of
CC root elongation caused by IAA-Leu or IAA-Ala.
CC {ECO:0000269|PubMed:15155875}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23796; AAC49016.1; -; mRNA.
DR EMBL; AF047031; AAC04866.1; -; Genomic_DNA.
DR EMBL; AB013392; BAB09884.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96793.1; -; Genomic_DNA.
DR EMBL; AY072084; AAL59907.1; -; mRNA.
DR RefSeq; NP_200477.1; NM_125049.3.
DR PDB; 1XMB; X-ray; 2.00 A; A=22-439.
DR PDB; 2Q43; X-ray; 2.00 A; A=22-439.
DR PDBsum; 1XMB; -.
DR PDBsum; 2Q43; -.
DR AlphaFoldDB; P54970; -.
DR SMR; P54970; -.
DR STRING; 3702.AT5G56660.1; -.
DR MEROPS; M20.014; -.
DR PaxDb; P54970; -.
DR PRIDE; P54970; -.
DR ProteomicsDB; 228838; -.
DR EnsemblPlants; AT5G56660.1; AT5G56660.1; AT5G56660.
DR GeneID; 835767; -.
DR Gramene; AT5G56660.1; AT5G56660.1; AT5G56660.
DR KEGG; ath:AT5G56660; -.
DR Araport; AT5G56660; -.
DR TAIR; locus:2164976; AT5G56660.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; P54970; -.
DR OMA; VNRCNAS; -.
DR OrthoDB; 1022341at2759; -.
DR PhylomeDB; P54970; -.
DR BioCyc; ARA:MON-4142; -.
DR BioCyc; MetaCyc:MON-4142; -.
DR EvolutionaryTrace; P54970; -.
DR PRO; PR:P54970; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P54970; baseline and differential.
DR Genevisible; P54970; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IDA:TAIR.
DR GO; GO:0010178; F:IAA-amino acid conjugate hydrolase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; IDA: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.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..439
FT /note="IAA-amino acid hydrolase ILR1-like 2"
FT /id="PRO_0000001190"
FT MOTIF 436..439
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54955,
FT ECO:0000305|PubMed:18543330"
FT CONFLICT 131
FT /note="A -> P (in Ref. 1; AAC49016)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="Q -> H (in Ref. 1; AAC49016)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="D -> G (in Ref. 5; AAL59907)"
FT /evidence="ECO:0000305"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1XMB"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:1XMB"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1XMB"
FT TURN 184..189
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 285..296
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 298..315
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:1XMB"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:2Q43"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:1XMB"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2Q43"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1XMB"
FT HELIX 408..427
FT /evidence="ECO:0007829|PDB:1XMB"
SQ SEQUENCE 439 AA; 47856 MW; BFA5F35AF4C4F508 CRC64;
MALNKLLSLT FQLLLFLLSV SSESPWIAED TSQIQTKLLE FAKSPEVFDW MVKIRRKIHE
NPELGYEELE TSKLIRSELE LIGIKYRYPV AITGVIGYIG TGEPPFVALR ADMDALPIQE
GVEWEHKSKI AGKMHACGHD GHVTMLLGAA KILHEHRHHL QGTVVLIFQP AEEGLSGAKK
MREEGALKNV EAIFGIHLSA RIPFGKAASR AGSFLAGAGV FEAVITGKGG HAAIPQHTID
PVVAASSIVL SLQQLVSRET DPLDSKVVTV SKVNGGNAFN VIPDSITIGG TLRAFTGFTQ
LQQRVKEVIT KQAAVHRCNA SVNLTPNGRE PMPPTVNNKD LYKQFKKVVR DLLGQEAFVE
AAPVMGSEDF SYFAETIPGH FSLLGMQDET NGYASSHSPL YRINEDVLPY GAAIHASMAV
QYLKEKASKG SVSGFHEEL
