ID   MIMC_MYCGD              Reviewed;         368 AA.
AC   E9RFT1;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Propane 2-monooxygenase, hydroxylase component small subunit {ECO:0000303|PubMed:21183637};
DE            EC=1.14.13.227 {ECO:0000305|PubMed:21183637};
DE   AltName: Full=Acetone 1-monooxygenase {ECO:0000303|PubMed:26293913};
DE   AltName: Full=Methylethylketone 1-monooxygenase {ECO:0000303|PubMed:26293913};
DE   AltName: Full=Phenol 4-monooxygenase {ECO:0000303|PubMed:21183637};
GN   Name=mimC {ECO:0000303|PubMed:21183637};
OS   Mycobacterium goodii (Mycolicibacterium goodii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=134601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A PROPANE 2-MONOOXYGENASE,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION BY ACETONE, AND
RP   SUBUNIT.
RC   STRAIN=12523 {ECO:0000312|EMBL:BAJ76720.1};
RX   PubMed=21183637; DOI=10.1128/aem.02316-10;
RA   Furuya T., Hirose S., Osanai H., Semba H., Kino K.;
RT   "Identification of the monooxygenase gene clusters responsible for the
RT   regioselective oxidation of phenol to hydroquinone in mycobacteria.";
RL   Appl. Environ. Microbiol. 77:1214-1220(2011).
RN   [2]
RP   INDUCTION BY MIMR.
RC   STRAIN=12523;
RX   PubMed=21856847; DOI=10.1128/jb.05525-11;
RA   Furuya T., Hirose S., Semba H., Kino K.;
RT   "Identification of the regulator gene responsible for the acetone-
RT   responsive expression of the binuclear iron monooxygenase gene cluster in
RT   mycobacteria.";
RL   J. Bacteriol. 193:5817-5823(2011).
RN   [3]
RP   FUNCTION AS A PHENOL 4-MONOOXYGENASE, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=12523;
RX   PubMed=23171424; DOI=10.1111/febs.12070;
RA   Furuya T., Hayashi M., Semba H., Kino K.;
RT   "The mycobacterial binuclear iron monooxygenases require a specific
RT   chaperonin-like protein for functional expression in a heterologous host.";
RL   FEBS J. 280:817-826(2013).
RN   [4]
RP   FUNCTION AS AN ACETONE 1-MONOOXYGENASE, CATALYTIC ACTIVITY, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=12523;
RX   PubMed=26293913; DOI=10.1093/femsle/fnv136;
RA   Furuya T., Nakao T., Kino K.;
RT   "Catalytic function of the mycobacterial binuclear iron monooxygenase in
RT   acetone metabolism.";
RL   FEMS Microbiol. Lett. 362:1-6(2015).
CC   -!- FUNCTION: Component of the propane 2-monooxygenase multicomponent
CC       enzyme system which is involved in the degradation of propane via the
CC       O2-dependent hydroxylation of propane (PubMed:21183637). Also involved
CC       in the degradation of acetone via the O2-dependent hydroxylation of
CC       acetone (PubMed:26293913). Also able to catalyze the oxidation of
CC       phenol, methylethylketone (2-butanone), 1-propanol and 2-propanol
CC       (PubMed:21183637, PubMed:23171424, PubMed:26293913).
CC       {ECO:0000269|PubMed:21183637, ECO:0000269|PubMed:23171424,
CC       ECO:0000269|PubMed:26293913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + propane = H2O + NAD(+) + propan-2-ol;
CC         Xref=Rhea:RHEA:49992, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17824, ChEBI:CHEBI:32879,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.227;
CC         Evidence={ECO:0000305|PubMed:21183637};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetone + H(+) + NADH + O2 = H2O + hydroxyacetone + NAD(+);
CC         Xref=Rhea:RHEA:55788, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27957,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000269|PubMed:26293913};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butan-2-one + H(+) + NADH + O2 = 1-hydroxy-2-butanone + H2O +
CC         NAD(+); Xref=Rhea:RHEA:55792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:28398, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:88390;
CC         Evidence={ECO:0000269|PubMed:26293913};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + phenol = H2O + hydroquinone + NAD(+);
CC         Xref=Rhea:RHEA:55796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:17594,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000269|PubMed:23171424, ECO:0000305|PubMed:21183637};
CC   -!- SUBUNIT: The propane 2-monooxygenase multicomponent enzyme system is
CC       composed of an electron transfer component and a monooxygenase
CC       component interacting with the effector protein MimD. The electron
CC       transfer component is composed of a reductase (MimB), and the
CC       monooxygenase component is formed by a large subunit (MimA) and a small
CC       subunit (MimC) (PubMed:21183637). Requires the presence of the
CC       chaperonin-like protein MimG to ensure a productive folding, resulting
CC       of a soluble MimC, which leads to the active form of MimABCD
CC       (PubMed:23171424). {ECO:0000305|PubMed:21183637,
CC       ECO:0000305|PubMed:23171424}.
CC   -!- INDUCTION: By acetone (PubMed:21183637). Transcriptionally activated by
CC       MimR (PubMed:21856847). {ECO:0000269|PubMed:21183637,
CC       ECO:0000269|PubMed:21856847}.
CC   -!- SIMILARITY: Belongs to the TmoE/XamoE family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB568291; BAJ76720.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9RFT1; -.
DR   SMR; E9RFT1; -.
DR   STRING; 134601.AFA91_29110; -.
DR   BioCyc; MetaCyc:MON-19804; -.
DR   BRENDA; 1.14.13.222; 13503.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd01058; AAMH_B; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012078; MP_mOase_hydro.
DR   InterPro; IPR003430; Phenol_Hydrox.
DR   InterPro; IPR012348; RNR-like.
DR   Pfam; PF02332; Phenol_Hydrox; 1.
DR   PIRSF; PIRSF000040; MMOH_comp; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   1: Evidence at protein level;
KW   Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..368
FT                   /note="Propane 2-monooxygenase, hydroxylase component small
FT                   subunit"
FT                   /id="PRO_0000442972"
SQ   SEQUENCE   368 AA;  41648 MW;  EA2672F90DFAB9F2 CRC64;
     MSAPEKPRER SFPKIEFTDS EAGAKVFPSS KSRSFSYFTP AKLRATMYED VTVDVQPDPD
     RHLTQGWIYG FGNGPGGYPK DWTTAKSSNW HAFLDPNEEW NQTIYRNNAA VVRQVELCLK
     NAKRARVYDG WHTIWLTFIE RHVGAWMHAE NGLALHVFTS IQRSGPTNMI NTAVAVNAAH
     KMRFAQDLAL FNLDLAEATD AFDGSVHRAV WQEAPEWQPT RRVVEELTAV GDWCQLLFAT
     NIVFEQLVGS LFRSELIMQI AARNGDYITP TIVGTGEHDY DRDLNYSRNL FRLLTRDPEH
     GEANKALFAE WLGIWVPRCL DAARALQPIW STPADKAVTF ASSLKAAKAK FSALLEEIDL
     DIPEELDK