ID   DMPL_PSEUF              Reviewed;         331 AA.
AC   P19730;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Phenol 2-monooxygenase, oxygenase component DmpL {ECO:0000305};
DE            EC=1.14.13.244 {ECO:0000269|PubMed:2254259};
DE   AltName: Full=Phenol 2-monooxygenase P1 component;
DE   AltName: Full=Phenol hydroxylase P1 protein;
GN   Name=dmpL {ECO:0000303|PubMed:2254258}; Synonyms=pheA2;
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, 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   -!- 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). DmpL 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 TmoE/XamoE family. {ECO:0000305}.
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DR   EMBL; M60276; AAA25940.1; -; Genomic_DNA.
DR   EMBL; D28864; BAA06015.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19730; -.
DR   SMR; P19730; -.
DR   BioCyc; MetaCyc:MON-12795; -.
DR   BRENDA; 1.14.13.244; 16277.
DR   UniPathway; UPA00728; -.
DR   GO; GO:0005727; C:extrachromosomal circular DNA; IDA:UniProtKB.
DR   GO; GO:0018662; F:phenol 2-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046191; P:aerobic phenol-containing compound catabolic process; IDA:UniProtKB.
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   Aromatic hydrocarbons catabolism; Monooxygenase; NAD; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..331
FT                   /note="Phenol 2-monooxygenase, oxygenase component DmpL"
FT                   /id="PRO_0000079942"
SQ   SEQUENCE   331 AA;  38208 MW;  8042F5723BE3A5E8 CRC64;
     MSVEIKTNTV DPIRQTYGNL QRRFGDKPAS RYQEASYDIE AVTNFHYRPL WDPQHELHDP
     TRTAIRMTDW HKVTDPRQFY YGAYVQTRAR MQEATEHAYG FCEKRELLSR LPAELQAKLL
     RCLVPLRHAE LGANMNNSSI AGDSIAATVT QMHIYQAMDR LGMGQYLSRI GLLLDGGTGE
     ALDQAKAYWL DDPIWQGLRR YVEDSFVIRD WFELGLAQNL VLDGLLQPLM YQRFDQWLTE
     NGGSDVAMLT EFMRDWYGES TRWVDAMFKT VLAENDANRE QVQAWLEVWE PRAYEALLPL
     AEEATGIAAL DEVRSAFATR LQKIGLKSRE E