ID   IAAH_ENTAG              Reviewed;         436 AA.
AC   O50173;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Indole-3-acetyl-aspartic acid hydrolase;
DE            EC=3.5.1.134 {ECO:0000269|PubMed:12226446};
DE   AltName: Full=IAA-Asp hydrolase;
GN   Name=iaaH;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14; 39-54;
RP   177-187; 334-352 AND 358-367, AND CHARACTERIZATION.
RC   STRAIN=GK12;
RX   PubMed=9747708; DOI=10.1007/s004380050802;
RA   Chou J.-C., Mulbry W.W., Cohen J.D.;
RT   "The gene for indole-3-acetyl-L-aspartic acid hydrolase from Enterobacter
RT   agglomerans: molecular cloning, nucleotide sequence, and expression in
RT   Escherichia coli.";
RL   Mol. Gen. Genet. 259:172-178(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12226446; DOI=10.1104/pp.112.3.1281;
RA   Chou J.C., Kuleck G.A., Cohen J.D., Mulbry W.W.;
RT   "Partial purification and characterization of an inducible indole-3-acetyl-
RT   L-aspartic acid hydrolase from Enterobacter agglomerans.";
RL   Plant Physiol. 112:1281-1287(1996).
CC   -!- FUNCTION: Hydrolyzes indole-3-acetyl-N-aspartic acid to indole-3-acetic
CC       acid. {ECO:0000269|PubMed:12226446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetyl-L-aspartate + H2O = (indol-3-yl)acetate +
CC         L-aspartate; Xref=Rhea:RHEA:60428, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30854, ChEBI:CHEBI:133482;
CC         EC=3.5.1.134; Evidence={ECO:0000269|PubMed:12226446};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.52 mM for (indol-3-yl)acetyl-L-aspartate
CC         {ECO:0000269|PubMed:12226446};
CC       pH dependence:
CC         Optimum pH is 8-8.5. {ECO:0000269|PubMed:12226446};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12226446}.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; AF006687; AAC61782.1; -; Genomic_DNA.
DR   PIR; T44439; T44439.
DR   AlphaFoldDB; O50173; -.
DR   SMR; O50173; -.
DR   MEROPS; M20.020; -.
DR   KEGG; ag:AAC61782; -.
DR   BRENDA; 3.5.1.134; 2084.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd05665; M20_Acy1_IAAspH; 1.
DR   InterPro; IPR033845; AbgA.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..436
FT                   /note="Indole-3-acetyl-aspartic acid hydrolase"
FT                   /id="PRO_0000061960"
SQ   SEQUENCE   436 AA;  46797 MW;  E72F8125CA6B0187 CRC64;
     MPLLNEYIRQ LLPEMTQWRR DLHHYAESGW VEFRTASKVA EQLHQLGYDL TLGRDAVDAD
     SRMGLPDEIT LANAFQRARE QGAPEPWLSA FEGGFTGIVA TLDTGRPGPT LAFRVDMDAL
     DLNEDTDGHH RPFREDFASC NPGMMHACGH DGHTAIGLGL AHVLKQYADR LHGVIKLIFQ
     PAEEGTRGAR AMVAAGVVDD VDYFTAIHIG TGVPAGTVVC GSDNFMATTK FDALFTGVAA
     HAGGKPEDGR NALLAAAQAA IALHAIAPHS AGASRVNVGV MQAGTGRNVV PSGALLKVET
     RGETEDINRY VFERAREVIH GAAAMYGASV ELRLMGAATS SAPSPGWVHY LREQAARVPG
     VEQAIDRIAA PAGSEDATLM MARVQQHNGL ASYMVFGTEL SAGHHNEQFD FDENVMAIAV
     ETLALTALNF PWQRGV