ID   PRMC_GORST              Reviewed;         368 AA.
AC   Q768T3;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Propane 2-monooxygenase, hydroxylase component small subunit {ECO:0000303|PubMed:14645271};
DE            Short=Prm {ECO:0000303|PubMed:14645271};
DE            EC=1.14.13.227 {ECO:0000305|PubMed:14645271};
DE   AltName: Full=Phenol 4-monooxygenase {ECO:0000303|PubMed:21183637};
GN   Name=prmC {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 AS A PROPANE 2-MONOOXYGENASE,
RP   CATALYTIC ACTIVITY, INDUCTION BY PROPANE, AND SUBUNIT.
RC   STRAIN=TY-5 {ECO:0000312|EMBL:BAD03958.1};
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   FUNCTION AS A PHENOL 4-MONOOXYGENASE, CATALYTIC ACTIVITY, AND INDUCTION BY
RP   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).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=TY-5;
RX   PubMed=23171424; DOI=10.1111/febs.12070;
RA   Furuya T., Hayashi M., Semba H., Kino K.;
RT   "The mycobacterial binuclear iron monooxygenases require a specific
RT   chaperonin-like protein for functional expression in a heterologous host.";
RL   FEBS J. 280:817-826(2013).
CC   -!- FUNCTION: Component of the propane 2-monooxygenase multicomponent
CC       enzyme system which is involved in the degradation of propane via the
CC       O2-dependent hydroxylation of propane (PubMed:14645271). Under acetone
CC       induction, also able to catalyze the oxidation of phenol to yield
CC       hydroquinone (PubMed:21183637). {ECO:0000269|PubMed:14645271,
CC       ECO:0000269|PubMed:21183637}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + propane = H2O + NAD(+) + propan-2-ol;
CC         Xref=Rhea:RHEA:49992, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17824, ChEBI:CHEBI:32879,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.227;
CC         Evidence={ECO:0000305|PubMed:14645271};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + phenol = H2O + hydroquinone + NAD(+);
CC         Xref=Rhea:RHEA:55796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:17594,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000305|PubMed:21183637};
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) (PubMed:14645271). Probably requires the presence of the
CC       chaperonin-like protein PrmG to ensure a productive folding, resulting
CC       of a soluble PrmC, which leads to the active form of PrmABCD
CC       (PubMed:23171424). {ECO:0000305|PubMed:14645271,
CC       ECO:0000305|PubMed:23171424}.
CC   -!- INDUCTION: By propane and acetone. {ECO:0000269|PubMed:14645271,
CC       ECO:0000269|PubMed:21183637}.
CC   -!- SIMILARITY: Belongs to the TmoE/XamoE family. {ECO:0000305}.
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DR   EMBL; AB112920; BAD03958.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q768T3; -.
DR   SMR; Q768T3; -.
DR   BioCyc; MetaCyc:MON-19809; -.
DR   BRENDA; 1.14.13.227; 7737.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd01058; AAMH_B; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012078; MP_mOase_hydro.
DR   InterPro; IPR003430; Phenol_Hydrox.
DR   InterPro; IPR012348; RNR-like.
DR   Pfam; PF02332; Phenol_Hydrox; 1.
DR   PIRSF; PIRSF000040; MMOH_comp; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   1: Evidence at protein level;
KW   Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..368
FT                   /note="Propane 2-monooxygenase, hydroxylase component small
FT                   subunit"
FT                   /id="PRO_0000442964"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  41946 MW;  84B977901E94F899 CRC64;
     MSAPAQPRER SFPSIEFTDA EADAREFPSS RSRKYNYYQP SKKRATIYED VTVDVQPDPE
     RHLTQGWIYG FGDGPGGYPK EWTSAQSSNW HQFLDPNEEW EQSIYRNNSA VVHQVDLCLQ
     NAKRARAYDG WNSAWLKFIE RNLGAWMHAE SGMGLHVFTS IQRSAPTNMI NNAVCVNAAH
     KLRFAQDLAL FNLDLSEAEE AFDGSAHKEV WQSAPEWQPT REAVERLTAI GDWAELLFCS
     NIVFEQLVGS LFRSELVMQV AARNGDYITP TIVGTGEYDY DRDLNYSRAL FQMLARDEKH
     GIDNRKLFSR WMSEWFPGAS TRARGLQPIW SQPADKSVTF SSSLEHAKTK FADVLAAIDV
     DIPEELNK