ID   Q98NA3_RHILO            Unreviewed;       475 AA.
AC   Q98NA3;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Indoleacetamide hydrolase {ECO:0000256|ARBA:ARBA00021874};
GN   OrderedLocusNames=mlr0229 {ECO:0000313|EMBL:BAB47858.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB47858.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB47858.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid
CC       (IAA). {ECO:0000256|ARBA:ARBA00003871}.
CC   -!- SIMILARITY: Belongs to the amidase family.
CC       {ECO:0000256|ARBA:ARBA00009199}.
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; BA000012; BAB47858.1; -; Genomic_DNA.
DR   RefSeq; WP_010909228.1; NC_002678.2.
DR   AlphaFoldDB; Q98NA3; -.
DR   KEGG; mlo:mlr0229; -.
DR   PATRIC; fig|266835.9.peg.178; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_4_5; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895:SF7; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
FT   DOMAIN          27..451
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   475 AA;  51240 MW;  BB36BD894945FF6E CRC64;
     MSDLDLCYMP AHEALRLFKA KKLSPVELMQ ATIRRAEATR SSINCFTFTH FEEAMKLAAR
     AEAKYARGAR AGALEGLPIG IKDESYIKGK PTSHGSLLSR DAIGGHTSTM NERIMKAGGI
     VHARTATPEF SCAGYTWSKR WGVTRNPWNP DFTPGGSSGG AAATLASGTS SIATGSDIAG
     SIRIPASACG LVGYKPPYGR NPDEPPFNLD FYCHTGPLAR NVRDAILLQN VMAGPSPLDI
     ATLRPKLRLP FDFKPIKGWR IAFSMDLGSF EVDPDVRKNT LAACDVFRSL GATVEEVDLG
     WDDGVLKAGM AYLEHLFGAS LSQLLAEHAK DMTSYARRFA EDGRKSKATD FVATLDVAAR
     MYQTLGPLLE TYDVLICPTN ALPAVPAEFD QTTDRVEING TEVNPSLGWV MTTPFNMLSR
     CPVLSIPSGH AASGVPTGIQ IVGRTYSDAD VFRAGLAYET ARGQWYGDTG TRPSL
//