PRMB_RHOJR
ID PRMB_RHOJR Reviewed; 370 AA.
AC Q0SJK8;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Propane 2-monooxygenase, reductase component {ECO:0000303|PubMed:17873074};
DE Short=PrMO {ECO:0000303|PubMed:17873074};
DE EC=1.18.1.- {ECO:0000305};
GN Name=prmB {ECO:0000303|PubMed:17873074};
GN OrderedLocusNames=RHA1_ro00442 {ECO:0000312|EMBL:ABG92278.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000312|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2]
RP FUNCTION, INDUCTION BY PROPANE, AND SUBUNIT.
RC STRAIN=RHA1;
RX PubMed=17873074; DOI=10.1128/aem.01697-07;
RA Sharp J.O., Sales C.M., LeBlanc J.C., Liu J., Wood T.K., Eltis L.D.,
RA Mohn W.W., Alvarez-Cohen L.;
RT "An inducible propane monooxygenase is responsible for N-
RT nitrosodimethylamine degradation by Rhodococcus sp. strain RHA1.";
RL Appl. Environ. Microbiol. 73:6930-6938(2007).
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:17873074}.
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 PrmD. The electron
CC transfer component is composed of a reductase (PrmB), and the
CC monooxygenase component is formed by a large subunit (PrmA) and a small
CC subunit (PrmC). {ECO:0000305|PubMed:17873074}.
CC -!- INDUCTION: By propane. {ECO:0000269|PubMed:17873074}.
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; CP000431; ABG92278.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SJK8; -.
DR SMR; Q0SJK8; -.
DR STRING; 101510.RHA1_ro00442; -.
DR EnsemblBacteria; ABG92278; ABG92278; RHA1_ro00442.
DR KEGG; rha:RHA1_ro00442; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_11; -.
DR OMA; FIKEFVV; -.
DR Proteomes; UP000008710; 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; 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 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..370
FT /note="Propane 2-monooxygenase, reductase component"
FT /id="PRO_0000442969"
FT DOMAIN 28..118
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 128..229
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 370 AA; 40978 MW; 8190AADB264AA9B8 CRC64;
MAPRPLRRHP PLHHSFHESR RDPVADKHRI NFEPVDIEME VGEDEYILDA AFRQGIHLMH
GCREGRCSAC KSFVLEGDIQ MEDYSTFACN DAEVDEGHVL LCRSTAYSDC TIELLNFDED
ELLGGVPIQD VRTRVTRIEP MTKDIVSLRL APVEPAGYEF KPGQYSDLHI PGTEEHRSFS
MATTRSTPGH VEFLIKKYPG GKFAGLLEDG ISVGDEIALT GPYGSFTIKE GHVLPMVFIG
GGAGMAPLLS LLRHMSETGN TRQVHFYYGA RTPQDLFYVD EILELGRGLT DFTFVACLSE
SMDPPPVGAI AVEDGNVTDV VGRREPDIGR AEVYLCGPPP MVDAALELLE ANGTPKDQIF
YDKFTSPAFE
