MIMB_MYCS2
ID MIMB_MYCS2 Reviewed; 348 AA.
AC A0QTU9; I7G6Z1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Propane 2-monooxygenase, reductase component {ECO:0000303|PubMed:21183637};
DE EC=1.18.1.- {ECO:0000305};
GN Name=mimB {ECO:0000303|PubMed:21183637};
GN OrderedLocusNames=MSMEG_1972 {ECO:0000312|EMBL:ABK70076.1},
GN MSMEI_1928 {ECO:0000312|EMBL:AFP38399.1};
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, INDUCTION BY ACETONE, AND SUBUNIT.
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.
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: Reductase 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. Reductase
CC catalyzes the transfer of electrons from NADH or NADPH to monooxygenase
CC (Probable). {ECO:0000269|PubMed:21183637}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q03304};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
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 bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70076.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38399.1; -; Genomic_DNA.
DR RefSeq; WP_011728054.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886337.1; NC_008596.1.
DR AlphaFoldDB; A0QTU9; -.
DR SMR; A0QTU9; -.
DR STRING; 246196.MSMEI_1928; -.
DR EnsemblBacteria; ABK70076; ABK70076; MSMEG_1972.
DR EnsemblBacteria; AFP38399; AFP38399; MSMEI_1928.
DR GeneID; 66733402; -.
DR KEGG; msg:MSMEI_1928; -.
DR KEGG; msm:MSMEG_1972; -.
DR PATRIC; fig|246196.19.peg.1949; -.
DR eggNOG; COG1018; Bacteria.
DR OMA; FIKEFVV; -.
DR OrthoDB; 1834577at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..348
FT /note="Propane 2-monooxygenase, reductase component"
FT /id="PRO_0000442945"
FT DOMAIN 5..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 105..206
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 348 AA; 38538 MW; DC901EC11ADECB0D CRC64;
MADSHKINFD PVDIEMEVRE DENILDAAFR QGIHLMHGCR EGRCSACKSY VLDGEIQMES
YSTFACNDAE VDEGYVLLCR SHAFSDCTIE LLNFDEDELL GGIPIQDVRT QVQAVEPKTR
DIVSLRLKPI EPGKFDFKPG QYADLHIPGT DEHRSFSMAT TQSRSDEVEF LIKKYPGGKF
SALLDGHIQV GDEIALTGPY GSFTLKDGHV LPVVCIGGGA GMAPILSLLR HMNETENSRP
ARFYYGARTP ADLFYLDEIL ELGKGIKDFR FIACLSESAD GEVPGRVTVE EGMVTDVVAR
HETAIAKTEV YLCGPPPMVD AALMFLDANC VPKDQVFYDS FTSPIFDQ
