PRMB_GORST
ID PRMB_GORST Reviewed; 346 AA.
AC Q768T4;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Propane 2-monooxygenase, reductase component {ECO:0000303|PubMed:14645271};
DE Short=Prm {ECO:0000303|PubMed:14645271};
DE EC=1.18.1.- {ECO:0000305};
GN Name=prmB {ECO:0000303|PubMed:14645271};
OS Gordonia sp. (strain TY-5).
OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX NCBI_TaxID=235467;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION BY PROPANE,
RP DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=TY-5 {ECO:0000312|EMBL:BAD03957.1};
RX PubMed=14645271; DOI=10.1128/jb.185.24.7120-7128.2003;
RA Kotani T., Yamamoto T., Yurimoto H., Sakai Y., Kato N.;
RT "Propane monooxygenase and NAD+-dependent secondary alcohol dehydrogenase
RT in propane metabolism by Gordonia sp. strain TY-5.";
RL J. Bacteriol. 185:7120-7128(2003).
RN [2]
RP DISRUPTION PHENOTYPE, AND INDUCTION BY ACETONE.
RC STRAIN=TY-5;
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).
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
CC (PubMed:14645271). Reductase catalyzes the transfer of electrons from
CC NADH or NADPH to monooxygenase (Probable).
CC {ECO:0000269|PubMed:14645271}.
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:14645271}.
CC -!- INDUCTION: By propane and acetone. {ECO:0000269|PubMed:14645271,
CC ECO:0000269|PubMed:21183637}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC propane and to catalyze the oxidation of phenol to yield hydroquinone.
CC {ECO:0000269|PubMed:14645271, ECO:0000269|PubMed:21183637}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD03957.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB112920; BAD03957.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q768T4; -.
DR SMR; Q768T4; -.
DR BioCyc; MetaCyc:MON-19808; -.
DR BRENDA; 1.14.13.227; 7737.
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; 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; 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..346
FT /note="Propane 2-monooxygenase, reductase component"
FT /id="PRO_0000442968"
FT DOMAIN 5..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 104..205
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 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 346 AA; 37719 MW; 1A0FBFEBE6BE49B4 CRC64;
MADTHKISFE PVDIEMEVGE DETILDAAFR QGIHLMHGCR EGRCSCKSYM LEGDVQMDDY
STFACNDAEE AEGYVLLCRT YAYSDCEIEL LNFDEDELLG GAPIQDVTTK VAAIEPMTPD
IVSLKLDVVE PESVEFKSGQ YFDLFIPGTE DKRSFSIATT PATPDRLEFL IKKYPGGLFA
GMLTDGLSVG QEIKLNGPYG SCTLRNGHVL PIVAIGGGAG MAPLLSLLRH ISETGLNRPV
RFYYGARTAA DLFLLDEIAT LGEKIDDFSF TACLSESTDN APEGVTVIGG NVTDIVNDNE
ADLARTEVYF CAPPPMVDAA LALAEQHSVP HDQIFYDKFT SPAFDS
