MIMB_MYCGD
ID MIMB_MYCGD Reviewed; 348 AA.
AC E9RFT0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
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};
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:BAJ76719.1};
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: 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; AB568291; BAJ76719.1; -; Genomic_DNA.
DR AlphaFoldDB; E9RFT0; -.
DR SMR; E9RFT0; -.
DR STRING; 134601.AFA91_29115; -.
DR BioCyc; MetaCyc:MON-19805; -.
DR BRENDA; 1.14.13.222; 13503.
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.
FT CHAIN 1..348
FT /note="Propane 2-monooxygenase, reductase component"
FT /id="PRO_0000442944"
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; 38088 MW; 793F2E1C5395AC50 CRC64;
MADSHKINFE PVDIEMDVRE DENILDAAFR QGIHLMHGCR EGRCSACKSY VLDGEIQMEN
YSTFACNDAE VDEGFVLLCR SHAFSDCTIE LLNFDEDELL GGIPIQDVRT EVLAVEPKTR
DIVSLRLKPV EPGKFDFKPG QYADLHIPGT EEHRSFSMAT TPSCSDEVEF LIKKYPGGKF
SALLDGHIQV GDEIALTGPY GSFTLKDGHV LPVVCIGGGA GMAPILSLLR HMNETGNGRP
ARFYYGARTA ADLFYLDEIL ELGKGIKDFQ FIACLSESAE GQVPGAVAVE EGMVTDVVAR
HESAIAKTEV YLCGPPPMVD AALGFLDANS VPKDQVFYDS FTSPIFDQ
