MIMA_MYCS2
ID MIMA_MYCS2 Reviewed; 542 AA.
AC A0QTU8; I7FI00;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Propane 2-monooxygenase, hydroxylase component large 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=mimA {ECO:0000303|PubMed:21183637};
GN OrderedLocusNames=MSMEG_1971 {ECO:0000312|EMBL:ABK75704.1},
GN MSMEI_1927 {ECO:0000312|EMBL:AFP38398.1};
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 {ECO:0000312|Proteomes:UP000000757};
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, DISRUPTION PHENOTYPE,
RP INDUCTION BY ACETONE, 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q00456};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q00456};
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 MimA, 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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC phenol, acetone and methylethylketone (2-butanone).
CC {ECO:0000269|PubMed:21183637}.
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; CP000480; ABK75704.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38398.1; -; Genomic_DNA.
DR RefSeq; WP_003893346.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886336.1; NC_008596.1.
DR AlphaFoldDB; A0QTU8; -.
DR SMR; A0QTU8; -.
DR STRING; 246196.MSMEI_1927; -.
DR EnsemblBacteria; ABK75704; ABK75704; MSMEG_1971.
DR EnsemblBacteria; AFP38398; AFP38398; MSMEI_1927.
DR GeneID; 66733401; -.
DR KEGG; msg:MSMEI_1927; -.
DR KEGG; msm:MSMEG_1971; -.
DR PATRIC; fig|246196.19.peg.1948; -.
DR eggNOG; COG3350; Bacteria.
DR OMA; RTGFTMQ; -.
DR OrthoDB; 147428at2; -.
DR BRENDA; 1.14.13.222; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..542
FT /note="Propane 2-monooxygenase, hydroxylase component large
FT subunit"
FT /id="PRO_0000442943"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
SQ SEQUENCE 542 AA; 63042 MW; 619741714018B9C4 CRC64;
MSRQSLTKAH AKISELTWEP TFATPATRFG TDYTFEKAPK KDPLKQIMRS YFSMEEEKDN
RVYGAMDGAI RGNMFRQVQQ RWLEWQKLFL SIIPFPEISA ARAMPMAIDA VPNPEIHNGL
AVQMIDEVRH STIQMNLKKL YMNNYIDPSG FDMTEKAFAN NYAGTIGRQF GEGFITGDAI
TAANIYLTVV AETAFTNTLF VAMPDEAAAN GDYLLPTVFH SVQSDESRHI SNGYSILLMA
LADERNRPLL ERDLRYAWWN NHCVVDAAIG TFIEYGTKDR RKDRESYAEM WRRWIYDDYY
RSYLLPLEKY GLTIPHDLVE EAWKRIVEKG YVHEVARFFA TGWPVNYWRI DTMTDTDFEW
FEHKYPGWYS KFGKWWENYN RLAYPGRNKP IAFEEVGYQY PHRCWTCMVP ALIREDMIVE
KVDGQWRTYC SETCYWTDAV AFRGEYEGRE TPNMGRLTGF REWETLHHGK DLADIVTDLG
YVRDDGKTLV GQPHLNLDPQ KMWTLDDVRG NTFNSPNVLL NQMTDDERDA HVAAYRAGGV
PA
