IACA_ACIB2
ID IACA_ACIB2 Reviewed; 389 AA.
AC D0C6T7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Indole-3-acetate monooxygenase {ECO:0000305};
DE EC=1.14.13.235 {ECO:0000250|UniProtKB:B0FXI0};
GN Name=iacA {ECO:0000303|PubMed:22311185};
GN ORFNames=HMPREF0010_00467 {ECO:0000312|EMBL:EEX04702.1};
OS Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG
OS 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=575584;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=22311185; DOI=10.1007/s10482-012-9704-4;
RA Lin G.H., Chen H.P., Huang J.H., Liu T.T., Lin T.K., Wang S.J., Tseng C.H.,
RA Shu H.Y.;
RT "Identification and characterization of an indigo-producing oxygenase
RT involved in indole 3-acetic acid utilization by Acinetobacter baumannii.";
RL Antonie Van Leeuwenhoek 101:881-890(2012).
CC -!- FUNCTION: Involved in the degradation of the plant hormone indole-3-
CC acetic acid (IAA) (PubMed:22311185). Catalyzes the first step of the
CC pathway, the conversion of IAA to 2-hydroxy-IAA (2-OH-IAA) (By
CC similarity). Can also convert indole to indoxyl, which spontaneously
CC dimerizes in the presence of oxygen to form the blue pigment indigo
CC (PubMed:22311185). {ECO:0000250|UniProtKB:B0FXI0,
CC ECO:0000269|PubMed:22311185}.
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:0000250|UniProtKB:B0FXI0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41212;
CC Evidence={ECO:0000250|UniProtKB:B0FXI0};
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:22311185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52837;
CC Evidence={ECO:0000269|PubMed:22311185};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.80 mM for indole {ECO:0000269|PubMed:22311185};
CC KM=0.25 mM for NADH {ECO:0000269|PubMed:22311185};
CC Note=kcat is 0.88 min(-1) with indole as substrate.
CC {ECO:0000269|PubMed:22311185};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:22311185};
CC -!- INDUCTION: Induced in the presence of IAA.
CC {ECO:0000269|PubMed:22311185}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot grow with IAA as the sole carbon
CC source. {ECO:0000269|PubMed:22311185}.
CC -!- SIMILARITY: Belongs to the HpaH/HsaA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; GG704572; EEX04702.1; -; Genomic_DNA.
DR EnsemblBacteria; EEX04702; EEX04702; HMPREF0010_00467.
DR BioCyc; ABAU575584-HMP:GM69-472-MON; -.
DR Proteomes; UP000005740; Unassembled WGS sequence.
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; IPR013786; AcylCoA_DH/ox_N.
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 Pfam; PF02771; Acyl-CoA_dh_N; 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_0000454113"
SQ SEQUENCE 389 AA; 42466 MW; 9D324722A085E531 CRC64;
MMNKLSKMEF AAQDKAVDLD ALCQEIRERA CAGEFDNQAY VSQDIIEKLK KIGVYRALVP
KRFGGEEWSP RQFCELIETL SKADGSVGWV ASFGMSPAYL GSLPEETLKE LYQNGPDVVF
AGGIFPPQPA EITDEGVVVR GRWKFSSGCM GADIVGVGIS PLKNNEMQGL PRMAVMPANK
AKIEMTWDTV GLKGTGSHDL VVEDVLVEKK WTFVRGEPSK LSEPFFKYPS LSLATQVLTV
VGIGVAAAAL EEFEKLAPGK ASITGGSEIA NRPVTQYEFA QADAEFQAAK SWFYQTMDIV
WNEIIAGREA TAEQISDMRL ACTHAARVCA KVTRKMQMLA GMTAIYTNNP FSRFVNDTNV
VTQHAFMGDA TLQNAGLVSF GLKPAPGYL
