HYIN_PSESS
ID HYIN_PSESS Reviewed; 455 AA.
AC P06618;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Indoleacetamide hydrolase;
DE Short=IAH;
DE EC=3.5.1.-;
DE AltName: Full=Indole-3-acetamide hydrolase;
GN Name=iaaH;
OS Pseudomonas savastanoi (Pseudomonas syringae pv. savastanoi).
OG Plasmid pIAA1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=29438;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EW2009;
RX PubMed=16593610; DOI=10.1073/pnas.82.19.6522;
RA Yamada T., Palm C.J., Brooks B., Kosuge T.;
RT "Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes
RT show homology with Agrobacterium tumefaciens T-DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6522-6526(1985).
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; M11035; AAA25853.1; -; Genomic_DNA.
DR PIR; B25493; B25493.
DR AlphaFoldDB; P06618; -.
DR SMR; P06618; -.
DR KEGG; ag:AAA25853; -.
DR BioCyc; MetaCyc:MON-7681; -.
DR UniPathway; UPA00151; -.
DR PHI-base; PHI:4171; -.
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; Plasmid.
FT CHAIN 1..455
FT /note="Indoleacetamide hydrolase"
FT /id="PRO_0000105250"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 170
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 48578 MW; 85999DD7684D0E53 CRC64;
MHEIITLESL CQALADGEIA AAELRERALD TEARLARLNC FIREGDAVSQ FGEADHAMKG
TPLWGMPVSF KDNICVRGLP LTAGTRGMSG FVSDQDAAIV SQLRALGAVV AGKNNMHELS
FGVTSINPHW GTVGNPVAPG YCAGGSSGGS AAAVASGIVP LSVGTDTGGS IRIPAAFCGI
TGFRPTTGRW STAGIIPVSH TKDCVGLLTR TAGDAGFLYG LLSGKQQSFP LSRTAPCRIG
LPVSMWSDLD GEVERACVNA LSLLRKTGFE FIEIDDADIV ELNQTLTFTV PLYEFFADLA
QSLLSLGWKH GIHHIFAQVD DANVKGIINH HLGEGAIKPA HYLSSLQNGE LLKRKMDELF
ARHNIELLGY PTVPCRVPHL DHADRPEFFS QAIRNTDLAS NAMLPSITIP VGPEGRLPVG
LSFDALRGRD ALLLSRVSAI EQVLGFVRKV LPHTT