ID   AMI1_ORYSJ              Reviewed;         435 AA.
AC   Q7XTK3;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Amidase 1 {ECO:0000303|PubMed:27135507};
DE            Short=OsAMI1 {ECO:0000303|PubMed:27135507};
DE            EC=3.5.1.4 {ECO:0000269|PubMed:27135507};
GN   Name=AMI1 {ECO:0000303|PubMed:27135507};
GN   OrderedLocusNames=Os04g0118100 {ECO:0000312|EMBL:BAF13970.1},
GN   LOC_Os04g02780 {ECO:0000305};
GN   ORFNames=OSJNBa0020P07.1 {ECO:0000312|EMBL:CAE01284.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
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 (Probable). Converts
CC       indole-3-acetamide (IAM) to indole-3-acetate, and phenyl-2-acetamide
CC       (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM
CC       (PubMed:27135507). {ECO:0000269|PubMed:27135507,
CC       ECO:0000305|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:27135507};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=375 pmol/sec/mg enzyme with indole-3-acetamide as substrate
CC         {ECO:0000269|PubMed:27135507};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:27135507};
CC       Temperature dependence:
CC         Optimum temperature is 27 degrees Celsius.
CC         {ECO:0000269|PubMed:27135507};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27135507}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:27135507}.
CC   -!- SIMILARITY: Belongs to the amidase 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; AL606450; CAE01284.1; -; Genomic_DNA.
DR   EMBL; AP008210; BAF13970.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS87628.1; -; Genomic_DNA.
DR   RefSeq; XP_015635920.1; XM_015780434.1.
DR   AlphaFoldDB; Q7XTK3; -.
DR   SMR; Q7XTK3; -.
DR   STRING; 4530.OS04T0118100-01; -.
DR   PaxDb; Q7XTK3; -.
DR   PRIDE; Q7XTK3; -.
DR   EnsemblPlants; Os04t0118100-01; Os04t0118100-01; Os04g0118100.
DR   GeneID; 4334958; -.
DR   Gramene; Os04t0118100-01; Os04t0118100-01; Os04g0118100.
DR   KEGG; osa:4334958; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_17_0_1; -.
DR   InParanoid; Q7XTK3; -.
DR   OMA; CVGPFAR; -.
DR   OrthoDB; 447457at2759; -.
DR   PlantReactome; R-OSA-1119388; IAA biosynthesis VI (via indole-3-acetamide).
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0004040; F:amidase activity; IDA:UniProtKB.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
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; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   1: Evidence at protein level;
KW   Auxin biosynthesis; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Amidase 1"
FT                   /id="PRO_0000442780"
FT   ACT_SITE        38
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q936X2"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q936X2"
FT   ACT_SITE        139
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q936X2"
SQ   SEQUENCE   435 AA;  46180 MW;  68962A7745ED2F45 CRC64;
     MAMAGGGRGD YGAFMERFVL PPPPSQQLPL HGLTFAIKDI FDIAGRVTGF GNPDWARTHA
     PAAATSPVVL AALAAGATSL GTTIMDEMAY SINGENTHYG TPTNPCAPGR VPGGSSSGSA
     VAVAANLVDF SLGTDTGGSV RVPAAYCGIF GLRPSHGLVS AENVIPMAQM FDTVGWFSRD
     LSTLSRVTKV LLPLPDDIVK QPTQVTIPMD CFQILGSLDD RTYQIINASV AKRFDSQILD
     NRNLGDFISD NVPSIGKFIT DFSESELPSV PALSVISHVM RGLQRSQFKA NHAEWVNTVK
     PNLGPGLRER ILEAIASGDN ESLEDFQAIR AEFKSALAAL LKDHGILAIP TVPGPPPKVG
     MEAAPLENFR ARAFSLLSIA GLSGFCQVSI PLGMRNGLPV SVSLVARHGA DHFLLNVVEE
     LYQTLIDEAT KTWSS