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Propane 2-monooxygenase, hydroxylase component large subunit (EC 1.14.13.227) (Acetone 1-monooxygenase) (Methylethylketone 1-monooxygenase) (Phenol 4-monooxygenase)

 MIMA_MYCS2              Reviewed;         542 AA.
A0QTU8; I7FI00;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 1.
23-MAY-2018, entry version 80.
RecName: Full=Propane 2-monooxygenase, hydroxylase component large subunit {ECO:0000303|PubMed:21183637};
EC=1.14.13.227 {ECO:0000305|PubMed:21183637};
AltName: Full=Acetone 1-monooxygenase {ECO:0000303|PubMed:26293913};
AltName: Full=Methylethylketone 1-monooxygenase {ECO:0000303|PubMed:26293913};
AltName: Full=Phenol 4-monooxygenase {ECO:0000303|PubMed:21183637};
Name=mimA {ECO:0000303|PubMed:21183637};
OrderedLocusNames=MSMEG_1971 {ECO:0000312|EMBL:ABK75704.1},
MSMEI_1927 {ECO:0000312|EMBL:AFP38398.1};
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium fortuitum complex.
NCBI_TaxID=246196;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000000757};
Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
Fraser C.M.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
"Interrupted coding sequences in Mycobacterium smegmatis: authentic
mutations or sequencing errors?";
Genome Biol. 8:R20.1-R20.9(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
PubMed=18955433; DOI=10.1101/gr.081901.108;
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
"Ortho-proteogenomics: multiple proteomes investigation through
orthology and a new MS-based protocol.";
Genome Res. 19:128-135(2009).
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION
PHENOTYPE, INDUCTION BY ACETONE, AND SUBUNIT.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=21183637; DOI=10.1128/AEM.02316-10;
Furuya T., Hirose S., Osanai H., Semba H., Kino K.;
"Identification of the monooxygenase gene clusters responsible for the
regioselective oxidation of phenol to hydroquinone in mycobacteria.";
Appl. Environ. Microbiol. 77:1214-1220(2011).
[5]
INDUCTION BY MIMR.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=21856847; DOI=10.1128/JB.05525-11;
Furuya T., Hirose S., Semba H., Kino K.;
"Identification of the regulator gene responsible for the acetone-
responsive expression of the binuclear iron monooxygenase gene cluster
in mycobacteria.";
J. Bacteriol. 193:5817-5823(2011).
[6]
FUNCTION AS A PHENOL 4-MONOOXYGENASE, AND CATALYTIC ACTIVITY.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=23892738; DOI=10.1128/AEM.01856-13;
Furuya T., Hayashi M., Kino K.;
"Reconstitution of active mycobacterial binuclear iron monooxygenase
complex in Escherichia coli.";
Appl. Environ. Microbiol. 79:6033-6039(2013).
[7]
FUNCTION AS A PHENOL 4-MONOOXYGENASE, CATALYTIC ACTIVITY, AND SUBUNIT.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=23171424; DOI=10.1111/febs.12070;
Furuya T., Hayashi M., Semba H., Kino K.;
"The mycobacterial binuclear iron monooxygenases require a specific
chaperonin-like protein for functional expression in a heterologous
host.";
FEBS J. 280:817-826(2013).
[8]
FUNCTION AS AN ACETONE 1-MONOOXYGENASE, CATALYTIC ACTIVITY, AND
SUBSTRATE SPECIFICITY.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=26293913; DOI=10.1093/femsle/fnv136;
Furuya T., Nakao T., Kino K.;
"Catalytic function of the mycobacterial binuclear iron monooxygenase
in acetone metabolism.";
FEMS Microbiol. Lett. 362:1-6(2015).
-!- FUNCTION: Component of the propane 2-monooxygenase multicomponent
enzyme system which is involved in the degradation of propane via
the O2-dependent hydroxylation of propane (PubMed:21183637). Also
involved in the degradation of acetone via the O2-dependent
hydroxylation of acetone (PubMed:26293913). Also able to catalyze
the oxidation of phenol, methylethylketone (2-butanone), 1-
propanol and 2-propanol (PubMed:21183637, PubMed:23892738,
PubMed:23171424, PubMed:26293913). {ECO:0000269|PubMed:21183637,
ECO:0000269|PubMed:23171424, ECO:0000269|PubMed:23892738,
ECO:0000269|PubMed:26293913}.
-!- CATALYTIC ACTIVITY: Propane + NADH + O(2) = propan-2-ol + NAD(+) +
H(2)O. {ECO:0000305|PubMed:21183637}.
-!- CATALYTIC ACTIVITY: Acetone + NADH + O(2) = acetol + NAD(+) +
H(2)O. {ECO:0000269|PubMed:26293913}.
-!- CATALYTIC ACTIVITY: Butan-2-one + NADH + O(2) = 1-hydroxy-2-
butanone + NAD(+) + H(2)O. {ECO:0000269|PubMed:26293913}.
-!- CATALYTIC ACTIVITY: Phenol + NADH + O(2) = hydroquinone + NAD(+) +
H(2)O. {ECO:0000269|PubMed:23171424, ECO:0000269|PubMed:23892738,
ECO:0000305|PubMed:21183637}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000250|UniProtKB:Q00456};
Note=Binds 2 Fe(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q00456};
-!- SUBUNIT: The propane 2-monooxygenase multicomponent enzyme system
is composed of an electron transfer component and a monooxygenase
component interacting with the effector protein MimD. The electron
transfer component is composed of a reductase (MimB), and the
monooxygenase component is formed by a large subunit (MimA) and a
small subunit (MimC) (PubMed:21183637). Requires the presence of
the chaperonin-like protein MimG to ensure a productive folding,
resulting of a soluble MimA, which leads to the active form of
MimABCD (PubMed:23171424). {ECO:0000269|PubMed:23171424,
ECO:0000305|PubMed:21183637}.
-!- INDUCTION: By acetone (PubMed:21183637). Transcriptionally
activated by MimR (PubMed:21856847). {ECO:0000269|PubMed:21183637,
ECO:0000269|PubMed:21856847}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
on phenol, acetone and methylethylketone (2-butanone).
{ECO:0000269|PubMed:21183637}.
-!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000480; ABK75704.1; -; Genomic_DNA.
EMBL; CP001663; AFP38398.1; -; Genomic_DNA.
RefSeq; WP_003893346.1; NZ_CP009494.1.
RefSeq; YP_886336.1; NC_008596.1.
STRING; 246196.MSMEG_1971; -.
EnsemblBacteria; ABK75704; ABK75704; MSMEG_1971.
EnsemblBacteria; AFP38398; AFP38398; MSMEI_1927.
GeneID; 4533884; -.
KEGG; msb:LJ00_09835; -.
KEGG; msg:MSMEI_1927; -.
KEGG; msm:MSMEG_1971; -.
PATRIC; fig|246196.19.peg.1948; -.
eggNOG; ENOG4105EUX; Bacteria.
eggNOG; ENOG410XRJ2; LUCA.
HOGENOM; HOG000076230; -.
KO; K18223; -.
OMA; DEFRHST; -.
OrthoDB; POG091H08A8; -.
Proteomes; UP000000757; Chromosome.
Proteomes; UP000006158; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
Gene3D; 1.10.620.20; -; 1.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR003430; Phenol_Hydrox.
InterPro; IPR012348; RNR-like.
Pfam; PF02332; Phenol_Hydrox; 1.
SUPFAM; SSF47240; SSF47240; 1.
1: Evidence at protein level;
Complete proteome; Iron; Metal-binding; Monooxygenase; NAD;
Oxidoreductase; Reference proteome.
CHAIN 1 542 Propane 2-monooxygenase, hydroxylase
component large subunit.
/FTId=PRO_0000442943.
METAL 97 97 Iron 1; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 127 127 Iron 1; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 127 127 Iron 2; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 130 130 Iron 1; via pros nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 192 192 Iron 2; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 226 226 Iron 1; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 226 226 Iron 2; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
METAL 229 229 Iron 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q00456}.
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


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