PRMA_RHOJR
ID PRMA_RHOJR Reviewed; 544 AA.
AC Q0SJK9;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Propane 2-monooxygenase, hydroxylase component large subunit {ECO:0000303|PubMed:17873074};
DE Short=PrMO {ECO:0000303|PubMed:17873074};
DE EC=1.14.13.227 {ECO:0000305|PubMed:17873074};
GN Name=prmA {ECO:0000303|PubMed:17873074};
GN OrderedLocusNames=RHA1_ro00441 {ECO:0000312|EMBL:ABG92277.1};
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, CATALYTIC ACTIVITY, INDUCTION BY PROPANE, DISRUPTION PHENOTYPE,
RP SUBSTRATE SPECIFICITY, 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).
RN [3]
RP SUBUNIT.
RC STRAIN=RHA1;
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. Also able to catalyze the
CC oxidation the water contaminant N-nitrosodimethylamine (NDMA).
CC {ECO:0000269|PubMed:17873074}.
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:17873074};
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:17873074). 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:17873074,
CC ECO:0000305|PubMed:23171424}.
CC -!- INDUCTION: By propane. {ECO:0000269|PubMed:17873074}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC propane and to degrade N-nitrosodimethylamine (NDMA).
CC {ECO:0000269|PubMed:17873074}.
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; CP000431; ABG92277.1; -; Genomic_DNA.
DR RefSeq; WP_011593714.1; NC_008268.1.
DR AlphaFoldDB; Q0SJK9; -.
DR SMR; Q0SJK9; -.
DR STRING; 101510.RHA1_ro00441; -.
DR EnsemblBacteria; ABG92277; ABG92277; RHA1_ro00441.
DR KEGG; rha:RHA1_ro00441; -.
DR PATRIC; fig|101510.16.peg.469; -.
DR eggNOG; COG3350; Bacteria.
DR HOGENOM; CLU_040795_0_0_11; -.
DR OMA; RTGFTMQ; -.
DR BRENDA; 1.14.13.227; 10764.
DR Proteomes; UP000008710; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..544
FT /note="Propane 2-monooxygenase, hydroxylase component large
FT subunit"
FT /id="PRO_0000442963"
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 544 AA; 63222 MW; 3A467FE3B4111CD2 CRC64;
MSRQSLTKAH AKITELSWDP TFATPATRFG TDYTFEKAPK KDPLKQIMRS YFPMEEEKDN
RVYGAMDGAI RGNMFRQVQQ RWLEWQKLFL SIIPFPEISA ARAMPMAIDA VPNPEIHNGL
AVQMIDEVRH STIQMNLKKL YMNNYIDPAG FDMTEKAFAN NYAGTIGRQF GEGFITGDAI
TAANIYLTVV AETAFTNTLF VAMPDEAAAN GDYLLPTVFH SVQSDESRHI SNGYSILLMA
LADERNRPLL ERDLRYAWWN NHCVVDAAIG TFIEYGTKDR RKDRESYAEM WRRWIYDDYY
RSYLIPLEKY GLTIPHDLVE EAWKRITDKG YVHEVARFFA TGWPVNYWRI DAMTDKDFEW
FEHKYPGWYS KYGKWWEEYN RLAYPGRNKP IAFEEVGYQY PHRCWTCMVP ALIREDMVVE
KVDDQWRTYC SETCYWTDAV AFRSEYQGRP TPNMGRLTGF REWETLHHGK DLADIVSDLG
YVRDDGKTLV GQPHLDLDDP KKMWTLDDVR GNTFQSPNVL LNEMSDAERN AHIAAYRAGG
AVPA
