ID   MIMD_MYCGD              Reviewed;         114 AA.
AC   E9RFT2;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Propane 2-monooxygenase, effector component {ECO:0000303|PubMed:21183637};
DE   AltName: Full=Propane 2-monooxygenase, coupling protein component {ECO:0000303|PubMed:21183637};
GN   Name=mimD {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, INDUCTION BY ACETONE, AND
RP   SUBUNIT.
RC   STRAIN=12523 {ECO:0000312|EMBL:BAJ76721.1};
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).
CC   -!- FUNCTION: Effector component of the propane 2-monooxygenase
CC       multicomponent enzyme system which is involved in the degradation of
CC       propane via the O2-dependent hydroxylation of propane.
CC       {ECO:0000269|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). {ECO:0000305|PubMed:21183637}.
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 TmoD/XamoD 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; BAJ76721.1; -; Genomic_DNA.
DR   RefSeq; WP_073678483.1; NZ_JAHBON010000026.1.
DR   AlphaFoldDB; E9RFT2; -.
DR   SMR; E9RFT2; -.
DR   STRING; 134601.AFA91_29105; -.
DR   BioCyc; MetaCyc:MON-19806; -.
DR   BRENDA; 1.14.13.222; 13503.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.56.10; -; 1.
DR   InterPro; IPR003454; MOase_MmoB_DmpM.
DR   InterPro; IPR036889; mOase_MmoB_DmpM_sf.
DR   Pfam; PF02406; MmoB_DmpM; 1.
DR   SUPFAM; SSF56029; SSF56029; 1.
PE   1: Evidence at protein level;
FT   CHAIN           1..114
FT                   /note="Propane 2-monooxygenase, effector component"
FT                   /id="PRO_0000442974"
SQ   SEQUENCE   114 AA;  12546 MW;  D96CE2877B238B22 CRC64;
     MSSMQFGAAT EFSNRCGVTL MNTPIGRVVA EVMGAKEGVE LTEYPSMIRV DGVKLLSFDY
     DELTDALGQE FDGSIFEEIS STHYGRMVHL DDKTMLFASP EDAAEYIGFD LTAQ