AMI1_ARATH
ID AMI1_ARATH Reviewed; 425 AA.
AC Q9FR37; O04032;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Amidase 1 {ECO:0000303|PubMed:16738862};
DE Short=AtAMI1 {ECO:0000303|PubMed:12620340};
DE EC=3.5.1.4 {ECO:0000269|PubMed:12620340, ECO:0000269|PubMed:17555521, ECO:0000269|PubMed:27135507};
DE AltName: Full=Translocon at the outer membrane of chloroplasts 64-I {ECO:0000305};
DE Short=AtTOC64-I {ECO:0000303|PubMed:14741350};
GN Name=AMI1 {ECO:0000303|PubMed:12620340};
GN Synonyms=TOC64-I {ECO:0000303|PubMed:14741350};
GN OrderedLocusNames=At1g08980 {ECO:0000312|Araport:AT1G08980};
GN ORFNames=F7G19.15 {ECO:0000312|EMBL:AAB70409.1};
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].
RA Chang W.Z., So M.W., Soll D.;
RT "Cloning and characterization of an amidase gene from Arabidopsis
RT thaliana.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12620340; DOI=10.1016/s0031-9422(02)00563-0;
RA Pollmann S., Neu D., Weiler E.W.;
RT "Molecular cloning and characterization of an amidase from Arabidopsis
RT thaliana capable of converting indole-3-acetamide into the plant growth
RT hormone, indole-3-acetic acid.";
RL Phytochemistry 62:293-300(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14741350; DOI=10.1016/s0014-5793(03)01457-1;
RA Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E.,
RA Millar A.H., Whelan J.;
RT "A plant outer mitochondrial membrane protein with high amino acid sequence
RT identity to a chloroplast protein import receptor.";
RL FEBS Lett. 557:109-114(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16738862; DOI=10.1007/s00425-006-0304-2;
RA Pollmann S., Neu D., Lehmann T., Berkowitz O., Schaefer T., Weiler E.W.;
RT "Subcellular localization and tissue specific expression of amidase 1 from
RT Arabidopsis thaliana.";
RL Planta 224:1241-1253(2006).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, AND MUTAGENESIS OF
RP LYS-36; SER-113; SER-114; ASP-133; SER-137; CYS-145 AND SER-214.
RX PubMed=17555521; DOI=10.1111/j.1742-4658.2007.05876.x;
RA Neu D., Lehmann T., Elleuche S., Pollmann S.;
RT "Arabidopsis amidase 1, a member of the amidase signature family.";
RL FEBS J. 274:3440-3451(2007).
RN [9]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17655652; DOI=10.1111/j.1365-313x.2007.03207.x;
RA Aronsson H., Boij P., Patel R., Wardle A., Toepel M., Jarvis P.;
RT "Toc64/OEP64 is not essential for the efficient import of proteins into
RT chloroplasts in Arabidopsis thaliana.";
RL Plant J. 52:53-68(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27135507; DOI=10.3390/plants3030324;
RA Sanchez-Parra B., Frerigmann H., Alonso M.M., Loba V.C., Jost R.,
RA Hentrich M., Pollmann S.;
RT "Characterization of four bifunctional plant IAM/PAM-amidohydrolases
RT capable of contributing to auxin biosynthesis.";
RL Plants (Basel) 3:324-347(2014).
CC -!- FUNCTION: Amidase involved in auxin biosynthesis. Converts indole-3-
CC acetamide to indole-3-acetate (PubMed:12620340, PubMed:27135507).
CC Converts phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate
CC preference is PAM > IAM (PubMed:27135507). Can also use L-asparagine
CC and 1-naphtalene-acetamide as substrates, but not indole-3-acetonitrile
CC or indole-3-acetyl-L-aspartic acid (PubMed:12620340).
CC {ECO:0000269|PubMed:12620340, ECO:0000269|PubMed:27135507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000269|PubMed:12620340, ECO:0000269|PubMed:17555521,
CC ECO:0000269|PubMed:27135507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12021;
CC Evidence={ECO:0000269|PubMed:12620340, ECO:0000269|PubMed:17555521,
CC ECO:0000269|PubMed:27135507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + indole-3-acetamide = (indol-3-yl)acetate + NH4(+);
CC Xref=Rhea:RHEA:34371, ChEBI:CHEBI:15377, ChEBI:CHEBI:16031,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30854; EC=3.5.1.4;
CC Evidence={ECO:0000269|PubMed:12620340};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34372;
CC Evidence={ECO:0000269|PubMed:12620340};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetamide + H2O = 2-phenylacetate + NH4(+);
CC Xref=Rhea:RHEA:64820, ChEBI:CHEBI:15377, ChEBI:CHEBI:16562,
CC ChEBI:CHEBI:18401, ChEBI:CHEBI:28938;
CC Evidence={ECO:0000269|PubMed:27135507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64821;
CC Evidence={ECO:0000269|PubMed:27135507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000269|PubMed:12620340};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017;
CC Evidence={ECO:0000269|PubMed:12620340};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-naphthaleneacetamide + H2O = 1-naphthaleneacetate + NH4(+);
CC Xref=Rhea:RHEA:64824, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:81810, ChEBI:CHEBI:156230;
CC Evidence={ECO:0000269|PubMed:12620340};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64825;
CC Evidence={ECO:0000269|PubMed:12620340};
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl fluoride (PMSF).
CC {ECO:0000269|PubMed:17555521}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=3.07 nmol/sec/mg enzyme with indole-3-acetamide as substrate
CC {ECO:0000269|PubMed:27135507};
CC pH dependence:
CC Optimum pH is 7.0 (PubMed:12620340). Optimum pH is 7.5
CC (PubMed:27135507). {ECO:0000269|PubMed:12620340,
CC ECO:0000269|PubMed:27135507};
CC Temperature dependence:
CC Optimum temperature is 35-37 degrees Celsius (PubMed:12620340,
CC PubMed:27135507). Optimum temperature is 37 degrees Celsius
CC (PubMed:27135507). {ECO:0000269|PubMed:12620340,
CC ECO:0000269|PubMed:27135507};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12620340,
CC ECO:0000269|PubMed:14741350, ECO:0000269|PubMed:16738862,
CC ECO:0000269|PubMed:27135507}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:27135507}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves and flower buds.
CC Lower levels in roots, stems and siliques.
CC {ECO:0000269|PubMed:12620340, ECO:0000269|PubMed:14741350,
CC ECO:0000269|PubMed:16738862, ECO:0000269|PubMed:17655652}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditioins. {ECO:0000269|PubMed:17655652}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF202077; AAG35612.1; -; mRNA.
DR EMBL; AC000106; AAB70409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28378.1; -; Genomic_DNA.
DR EMBL; AY037198; AAK59783.1; -; mRNA.
DR EMBL; BT004554; AAO42800.1; -; mRNA.
DR PIR; F86221; F86221.
DR RefSeq; NP_563831.1; NM_100769.4.
DR AlphaFoldDB; Q9FR37; -.
DR SMR; Q9FR37; -.
DR STRING; 3702.AT1G08980.1; -.
DR iPTMnet; Q9FR37; -.
DR PaxDb; Q9FR37; -.
DR PRIDE; Q9FR37; -.
DR ProteomicsDB; 245071; -.
DR EnsemblPlants; AT1G08980.1; AT1G08980.1; AT1G08980.
DR GeneID; 837418; -.
DR Gramene; AT1G08980.1; AT1G08980.1; AT1G08980.
DR KEGG; ath:AT1G08980; -.
DR Araport; AT1G08980; -.
DR TAIR; locus:2036029; AT1G08980.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_17_0_1; -.
DR InParanoid; Q9FR37; -.
DR OMA; TVGWMTR; -.
DR OrthoDB; 447457at2759; -.
DR PhylomeDB; Q9FR37; -.
DR BioCyc; ARA:AT1G08980-MON; -.
DR BioCyc; MetaCyc:AT1G08980-MON; -.
DR PRO; PR:Q9FR37; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FR37; baseline and differential.
DR Genevisible; Q9FR37; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0004040; F:amidase activity; IDA:TAIR.
DR GO; GO:0004067; F:asparaginase activity; IEA:RHEA.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:TAIR.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IDA:TAIR.
DR GO; GO:0009851; P:auxin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IDA:TAIR.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 2.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Auxin biosynthesis; Cytoplasm; Hydrolase; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..425
FT /note="Amidase 1"
FT /id="PRO_0000414025"
FT ACT_SITE 36
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17555521"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17555521"
FT ACT_SITE 137
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000269|PubMed:17555521"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 36
FT /note="K->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 36
FT /note="K->R: Reduces catalytic activity 10-fold."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 113
FT /note="S->A,T: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 114
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 114
FT /note="S->T: Reduces catalytic activity 400-fold."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 133
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 133
FT /note="D->E: Reduces catalytic activity 600-fold."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 137
FT /note="S->A: Reduces catalytic activity 170-fold."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 137
FT /note="S->T: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 145
FT /note="C->A,S: Reduces catalytic activity 10-fold."
FT /evidence="ECO:0000269|PubMed:17555521"
FT MUTAGEN 214
FT /note="S->T: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:17555521"
SQ SEQUENCE 425 AA; 45056 MW; 32849F5A1E542249 CRC64;
MATNNDFGAF IEKVTISPTS TSSSPPSLQG LTFAIKDIFD VEGRVTGFGN PDWLRTHSAA
TSTAPVVSSL LEAGATALGI TIMDEMAYSI NGENAHYGTP RNPIAFDRVP GGSSSGSAVA
VAARLVDFSI GTDTGGSVRV PASYCGIFGF RPSHGAVSTV GLTPMAQSFD TVGWFARDTA
TLKRVGCVLL QQHHLNPIEP SQLIIADDCF KLCSVPHDLL VQPLVGSVEK SFGGNTVVKK
VNLGEYIGQN VPSLKHFMTS DDVTTQQEFC IPSLMALSSS MRLLQRHEFK INHGAWISSV
KPEFGPGISE RIEEAIRTSD EKIDHCRSVK SELITALSTL LGEKGVLVIP TVPGPPPHLQ
ANVAALESFR SRAFSLLSIA GVSGFCQVSI PLGLHENLPV SVSLVAKYGS DGFLLSLVDS
LAAFI
