ID   IACA_PSEPU              Reviewed;         389 AA.
AC   B0FXI0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Indole-3-acetate monooxygenase {ECO:0000305};
DE            EC=1.14.13.235 {ECO:0000269|PubMed:23881445};
GN   Name=iacA {ECO:0000303|PubMed:18205812};
GN   ORFNames=E6B08_12580 {ECO:0000312|EMBL:QCI12141.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=1290;
RX   PubMed=18205812; DOI=10.1111/j.1574-6941.2008.00436.x;
RA   Leveau J.H.J., Gerards S.;
RT   "Discovery of a bacterial gene cluster for catabolism of the plant hormone
RT   indole 3-acetic acid.";
RL   FEMS Microbiol. Ecol. 65:238-250(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1290;
RA   Laird T.S., Leveau J.H.J.;
RT   "Genome sequence of Pseudomonas putida 1290, an auxin catabolizing
RT   strain.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=1290;
RX   PubMed=23881445; DOI=10.1007/s10886-013-0324-x;
RA   Scott J.C., Greenhut I.V., Leveau J.H.;
RT   "Functional characterization of the bacterial iac genes for degradation of
RT   the plant hormone indole-3-acetic acid.";
RL   J. Chem. Ecol. 39:942-951(2013).
CC   -!- FUNCTION: Involved in the degradation of the plant hormone indole-3-
CC       acetic acid (IAA) (PubMed:18205812, PubMed:23881445). Catalyzes the
CC       first step of the pathway, the conversion of IAA to 2-hydroxy-IAA (2-
CC       OH-IAA) (PubMed:23881445). Can also convert indole to indoxyl, which
CC       spontaneously dimerizes in the presence of oxygen to form the blue
CC       pigment indigo (PubMed:23881445). {ECO:0000269|PubMed:18205812,
CC       ECO:0000269|PubMed:23881445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetate + H(+) + NADH + O2 = 2-hydroxy-(1H-indol-
CC         3-yl)acetate + H2O + NAD(+); Xref=Rhea:RHEA:41211, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30854,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:136436;
CC         EC=1.14.13.235; Evidence={ECO:0000269|PubMed:23881445};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41212;
CC         Evidence={ECO:0000269|PubMed:23881445};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + indole + NADH + O2 = H2O + indoxyl + NAD(+);
CC         Xref=Rhea:RHEA:52836, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16881, ChEBI:CHEBI:17840,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000269|PubMed:23881445};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52837;
CC         Evidence={ECO:0000269|PubMed:23881445};
CC   -!- INDUCTION: Induced in the presence of IAA. Expression is probably
CC       repressed by IacR and exposure to IAA relieves this repression.
CC       {ECO:0000269|PubMed:23881445}.
CC   -!- MISCELLANEOUS: Transformation of P.putida KT2440, which cannot degrade
CC       IAA, with the iac gene cluster confers the ability to grow on IAA as a
CC       sole source of carbon and energy, but not the ability to chemotaxis
CC       towards IAA. {ECO:0000269|PubMed:23881445}.
CC   -!- SIMILARITY: Belongs to the HpaH/HsaA monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; EU360594; ABY62757.1; -; Genomic_DNA.
DR   EMBL; CP039371; QCI12141.1; -; Genomic_DNA.
DR   EnsemblBacteria; QCI12141; QCI12141; E6B08_12580.
DR   BioCyc; MetaCyc:MON-18108; -.
DR   BRENDA; 1.14.13.235; 5092.
DR   Proteomes; UP000298551; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..389
FT                   /note="Indole-3-acetate monooxygenase"
FT                   /id="PRO_0000454114"
SQ   SEQUENCE   389 AA;  41423 MW;  197FAD3AB5D84263 CRC64;
     MDSLCLRAAP ASALASGPAF EALLDGVRDR ARLGEFDRQR HISRDVIDAF KAHGVYRALV
     PKRFGGLECS PAAFCEMIER ISHADGSAGW VASFGMSPVY LAALPLETIA EIYGNSPDTV
     FAGGIFPPQA AEIVSGGFKI NGRWKYSSGS MGADIVGVGI APRNGDKLDL PRLAVLPRSQ
     ARIEETWDTV GLLGTGSHDL VVEDVVVGEQ WTFVRGGKPN LDEPFFRYPS LSFATQVLSV
     VGLGIARAAL DELSGMASGR ISVTGAPALA DRPLAQVDVA KAEAALRSAR AFFYESIERA
     WEHVLAGDPV PVDVTNLLRL SSTHAARVAA EVARSAQMLS GMTGIYNESP LARCVNDAQV
     VTQHAFMGDV TYQNAGAMFF GKQPLPGYL