DMPN_PSEUF
ID DMPN_PSEUF Reviewed; 517 AA.
AC P19732;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Phenol 2-monooxygenase, oxygenase component DmpN {ECO:0000305};
DE EC=1.14.13.244 {ECO:0000269|PubMed:2254259};
DE AltName: Full=Phenol 2-monooxygenase P3 component;
DE AltName: Full=Phenol hydroxylase P3 protein;
GN Name=dmpN {ECO:0000303|PubMed:2254258}; Synonyms=pheA4;
OS Pseudomonas sp. (strain CF600).
OG Plasmid pVI150.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=79676;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CF600;
RX PubMed=2254258; DOI=10.1128/jb.172.12.6826-6833.1990;
RA Nordlund I., Powlowski J., Shingler V.;
RT "Complete nucleotide sequence and polypeptide analysis of multicomponent
RT phenol hydroxylase from Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 172:6826-6833(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BH;
RA Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=CF600;
RX PubMed=2254259; DOI=10.1128/jb.172.12.6834-6840.1990;
RA Powlowski J., Shingler V.;
RT "In vitro analysis of polypeptide requirements of multicomponent phenol
RT hydroxylase from Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 172:6834-6840(1990).
RN [4]
RP INTERACTION WITH DMPK.
RC STRAIN=CF600;
RX PubMed=8995386; DOI=10.1074/jbc.272.2.945;
RA Powlowski J., Sealy J., Shingler V., Cadieux E.;
RT "On the role of DmpK, an auxiliary protein associated with multicomponent
RT phenol hydroxylase from Pseudomonas sp. strain CF600.";
RL J. Biol. Chem. 272:945-951(1997).
RN [5]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=CF600;
RX PubMed=12186554; DOI=10.1021/bi025901u;
RA Cadieux E., Vrajmasu V., Achim C., Powlowski J., Muenck E.;
RT "Biochemical, Moessbauer, and EPR studies of the diiron cluster of phenol
RT hydroxylase from Pseudomonas sp. strain CF 600.";
RL Biochemistry 41:10680-10691(2002).
CC -!- FUNCTION: Part of a multicomponent enzyme which catalyzes the
CC degradation of phenol and some of its methylated derivatives
CC (PubMed:2254259). DmpL, DmpN and DmpO form the oxygenase component of
CC the complex (PubMed:12186554). Required for growth on phenol and for in
CC vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
CC {ECO:0000269|PubMed:12186554, ECO:0000269|PubMed:2254258,
CC ECO:0000269|PubMed:2254259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + phenol = catechol + H2O + NAD(+);
CC Xref=Rhea:RHEA:57952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:18135,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.244;
CC Evidence={ECO:0000269|PubMed:2254259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57953;
CC Evidence={ECO:0000269|PubMed:2254259};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:12186554};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000269|PubMed:12186554};
CC -!- ACTIVITY REGULATION: Requires DmpM for efficient turnover. The activity
CC of DmpLNO oxygenase is inhibited by dithiothreitol (DTT) by a mechanism
CC apparently involving H(2)O(2) generation.
CC {ECO:0000269|PubMed:12186554}.
CC -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC {ECO:0000269|PubMed:2254258}.
CC -!- SUBUNIT: The multicomponent enzyme phenol hydroxylase is formed by DmpL
CC (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4
CC component) and DmpP (P5 component) (PubMed:2254259). The oxygenase
CC component is a dimer composed of three subunits, DmpL, DmpN and DmpO
CC (DmpLNO) (PubMed:12186554). DmpN interacts with the auxiliary protein
CC DmpK (P0 component) (PubMed:8995386). {ECO:0000269|PubMed:12186554,
CC ECO:0000269|PubMed:2254259, ECO:0000269|PubMed:8995386}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on phenol.
CC {ECO:0000269|PubMed:2254258}.
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; M60276; AAA25942.1; -; Genomic_DNA.
DR EMBL; D28864; BAA06017.1; -; Genomic_DNA.
DR AlphaFoldDB; P19732; -.
DR SMR; P19732; -.
DR BioCyc; MetaCyc:MON-12797; -.
DR BRENDA; 1.14.13.244; 16277.
DR UniPathway; UPA00728; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR007029; YHS_dom.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR Pfam; PF04945; YHS; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Iron; Metal-binding; Monooxygenase; NAD;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..517
FT /note="Phenol 2-monooxygenase, oxygenase component DmpN"
FT /id="PRO_0000079945"
FT BINDING 109
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 139
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 139
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 142
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 200
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 234
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 234
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 237
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 517 AA; 60523 MW; 4EFD4EB40ED73F9C CRC64;
MATHNKKRLN LKDKYRYLTR DLAWETTYQK KEDVFPLEHF EGIKITDWDK WEDPFRLTMD
TYWKYQAEKE KKLYAIFDAF AQNNGHQNIS DARYVNALKL FLTAVSPLEY QAFQGFSRVG
RQFSGAGARV ACQMQAIDEL RHVQTQVHAM SHYNKHFDGL HDFAHMYDRV WYLSVPKSYM
DDARTAGPFE FLTAVSFSFE YVLTNLLFVP FMSGAAYNGD MATVTFGFSA QSDEARHMTL
GLEVIKFMLE QHEDNVPIIQ RWIDKWFWRG YRLLTLIGMM MDYMLPNKVM SWSEAWGVYF
EQAGGALFKD LERYGIRPPK YVEQTTIGKE HITHQVWGAL YQYSKATSFH TWIPGDEELN
WLSEKYPDTF DKYYRPRFEF WREQQAKGER FYNDTLPHLC QVCQLPVIFT EPDDPTKLSL
RSLVHEGERY QFCSDGCCDI FKNEPVKYIQ AWLPVHQIYQ GNCEGGDVET VVQKYYHIKS
GVDNLEYLGS PEHQRWLALK GQTPPTAAPA DKSLGAA
