PRMA_GORST
ID PRMA_GORST Reviewed; 545 AA.
AC Q768T5;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Propane 2-monooxygenase, hydroxylase component large 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=prmA {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:BAD03956.2};
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q00456};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q00456};
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 PrmA, 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 TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; AB112920; BAD03956.2; -; Genomic_DNA.
DR AlphaFoldDB; Q768T5; -.
DR SMR; Q768T5; -.
DR BioCyc; MetaCyc:MON-19810; -.
DR BRENDA; 1.14.13.227; 7737.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..545
FT /note="Propane 2-monooxygenase, hydroxylase component large
FT subunit"
FT /id="PRO_0000442962"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
SQ SEQUENCE 545 AA; 63414 MW; FF69DC45D5F7AD3F CRC64;
MSRQSLTKAH AKITELSWEP TFATPATRFG TDYTFEKAPK KDPLKQIMRS YFPMEEEKDN
RVYGAMDGAI RGNMFRQVQE RWLEWQKLFL SIIPFPEISA ARAMPMAIDA VPNPEIHNGL
AVQMIDEVRH STIQMNLKKL YMNNYIDPAG FDITEKAFAN NYAGTIGRQF GEGFITGDAI
TAANIYLTVV AETAFTNTLF VAMPDEAAAN GDYLLPTVFH SVQSDESRHI SNGYSILLMA
LADERNRPLL ERDLRYAWWN NHCVVDAAIG TFIEYGTKDR RKDRESYAEM WRRWIYDDYY
RSYLLPLEKY GLTIPHDLVE EAWNRIVDKH YVHEVARFFA TGWPVNYWRI DAMTDTDFEW
FEEKYPGWYN KFGKWWENYN RLAYPGKNKP IAFEDVDYEY PHRCWTCMVP CLIREDMVTD
KVDGQWRTYC SETCAWTDKV AFRPEYEGRP TPNMGRLTGF REWETLHHGK DLADIITDLG
YVRDDGKTLI PQPHLDLDPK KMWTLDDVRG IPFGSPNVAL NEMSDDEREA HIAAYMANKN
GAVTV
