MIMC_MYCS2
ID MIMC_MYCS2 Reviewed; 368 AA.
AC I7FA35;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 25-MAY-2022, entry version 21.
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};
GN OrderedLocusNames=MSMEG_1973, MSMEI_1929 {ECO:0000312|EMBL:AFP38400.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION BY ACETONE,
RP AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [5]
RP INDUCTION BY MIMR.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [6]
RP FUNCTION AS A PHENOL 4-MONOOXYGENASE, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23892738; DOI=10.1128/aem.01856-13;
RA Furuya T., Hayashi M., Kino K.;
RT "Reconstitution of active mycobacterial binuclear iron monooxygenase
RT complex in Escherichia coli.";
RL Appl. Environ. Microbiol. 79:6033-6039(2013).
RN [7]
RP FUNCTION AS A PHENOL 4-MONOOXYGENASE, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [8]
RP FUNCTION AS AN ACETONE 1-MONOOXYGENASE, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 700084 / mc(2)155;
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:23892738, PubMed:23171424, PubMed:26293913).
CC {ECO:0000269|PubMed:21183637, ECO:0000269|PubMed:23171424,
CC ECO:0000269|PubMed:23892738, 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:0000269|PubMed:23892738,
CC 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:0000269|PubMed:23171424,
CC 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 TmoE/XamoE family. {ECO:0000305}.
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DR EMBL; CP000480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001663; AFP38400.1; -; Genomic_DNA.
DR RefSeq; WP_014877261.1; NZ_SIJM01000020.1.
DR AlphaFoldDB; I7FA35; -.
DR SMR; I7FA35; -.
DR STRING; 246196.MSMEI_1929; -.
DR EnsemblBacteria; AFP38400; AFP38400; MSMEI_1929.
DR GeneID; 66733403; -.
DR KEGG; msg:MSMEI_1929; -.
DR OrthoDB; 561064at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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; Reference proteome.
FT CHAIN 1..368
FT /note="Propane 2-monooxygenase, hydroxylase component small
FT subunit"
FT /id="PRO_0000442973"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41642 MW; 3EE4A933CF20A5C3 CRC64;
MSAPEKPRER SFPKIEFTDS EAGAKEFPSS KSRSYSYFTP AKLRATMYED VTVDVQPDPD
RHLTQGWIYG FGNGPGGYPK DWTTAKSSDW HAFRDPNEEW NQTIYRNNAA VVRQVELCLK
NAKRARVYDG WNSTWLTFIE RNVGAWMHAE NGLALHVFTS IQRSGPTNMI NTAVAVNAAH
KMRFAQDLAL FNLDLAEATE AFDGSAHRAV WQEAREWQAT RKVVEELTAV GDWCQLLFAT
NIVFEQLVGS LFRTELIMQI AARNGDYITP TIVGTGEHDY DRDLNYTRNL FRLLTRDPEH
GEANKALFTE WLGIWVPRCL DAALALQPIW SAPADKAVTF ASSLDAAKAK FTALLEEIDL
DIPEELNK
