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HYIN_BRAJP
ID   HYIN_BRAJP              Reviewed;         465 AA.
AC   P19922;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Indoleacetamide hydrolase;
DE            Short=IAH;
DE            EC=3.5.1.-;
DE   AltName: Full=Indole-3-acetamide hydrolase;
GN   Name=bam;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J1063;
RX   PubMed=2771653; DOI=10.1093/nar/17.15.6400;
RA   Sekine M., Watanabe K., Syono K.;
RT   "Nucleotide sequence of a gene for indole-3-acetamide hydrolase from
RT   Bradyrhizobium japonicum.";
RL   Nucleic Acids Res. 17:6400-6400(1989).
CC   -!- FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid
CC       (IAA).
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; X15117; CAA33213.1; -; Genomic_DNA.
DR   EMBL; M24333; AAA26220.1; -; Genomic_DNA.
DR   PIR; S05311; S05311.
DR   AlphaFoldDB; P19922; -.
DR   SMR; P19922; -.
DR   STRING; 1304878.AUGD01000004_gene4954; -.
DR   eggNOG; COG0154; Bacteria.
DR   UniPathway; UPA00151; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Auxin biosynthesis; Hydrolase.
FT   CHAIN           1..465
FT                   /note="Indoleacetamide hydrolase"
FT                   /id="PRO_0000105247"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  50266 MW;  4B337BE0BBD60740 CRC64;
     MVRGRHRSRD PQRRDLRGRD RRSASRTDAR RQSAAERGCR RSQRGSAEGC ACGRQTGPRA
     ARSACCTACP SRSRRMSTTE GRPNFNGVPA NKDFVAPSDS PVVHNLKKAG AIVIGLTNTP
     EFSFRGFTDN PLHGLTLNPW DPNITCGGSS GGAGSAVAAG IGTIAHGNDI GGSLRWPAHC
     NGVATIKPTQ GRIPAFNGSA TAERPMLAHL MSAQGPLARH VGDVRLALDV MSQADPRDPW
     WVPAPLAGPR PKGPIKVALA RIPEDMDVDP SVRAALRQAA DHLERSGYRV TEVDVPDIDG
     VWQTWCDIIT NETVVMQEAG MLKVTSEDFH KAWGGMKTKA NVLDLKAWMQ ATAARNGHIR
     AWQLFFEEYP VVLAPTTVKP TPGPRDDTVS ADRVKEIFWG EIRFISAINV LGLPGAVVPV
     TLHDGKPIGV QLIAGRYRED LALDAAAAIE KRAGVLAHRL WETME
 
 
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