DMPP_PSEUF
ID DMPP_PSEUF Reviewed; 353 AA.
AC P19734;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phenol 2-monooxygenase, reductase component DmpP {ECO:0000305};
DE EC=1.14.13.244 {ECO:0000269|PubMed:2254259};
DE AltName: Full=Phenol 2-monooxygenase P5 component;
DE AltName: Full=Phenol hydroxylase P5 protein;
GN Name=dmpP {ECO:0000303|PubMed:2254258};
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 PROTEIN SEQUENCE OF 2-5, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP 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).
CC -!- FUNCTION: Part of a multicomponent enzyme which catalyzes the
CC degradation of phenol and some of its methylated derivatives
CC (PubMed:2254259). DmpP probably transfers electrons from NADH, via FAD
CC and the iron-sulfur center, to the oxygenase component of the complex
CC (PubMed:2254259). Required for growth on phenol and for in vitro phenol
CC hydroxylase activity (PubMed:2254258, PubMed:2254259).
CC {ECO:0000269|PubMed:2254258, 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:2254259};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:2254259};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:2254259};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:2254259};
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). {ECO:0000269|PubMed:2254259}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on phenol.
CC {ECO:0000269|PubMed:2254258}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60276; AAA25944.1; -; Genomic_DNA.
DR AlphaFoldDB; P19734; -.
DR SMR; P19734; -.
DR BioCyc; MetaCyc:MON-12799; -.
DR BRENDA; 1.14.13.244; 16277.
DR UniPathway; UPA00728; -.
DR GO; GO:0005727; C:extrachromosomal circular DNA; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Monooxygenase; NAD; Oxidoreductase; Plasmid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2254259"
FT CHAIN 2..353
FT /note="Phenol 2-monooxygenase, reductase component DmpP"
FT /id="PRO_0000189407"
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 102..201
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 353 AA; 38478 MW; 007E85A5DF189CD0 CRC64;
MSYNVTIEPT GEVIEVEDGQ TILQAALRQG VWLPFACGHG TCATCKVQVV EGEVDIGEAS
PFALMDIERD ERKVLACCAI PLSDLVIEAD VDADPDFLGH PVEDYRGVVS ALVDLSPTIK
GLHIKLDRPM PFQAGQYVNL ALPGIDGTRA FSLANPPSRN DEVELHVRLV EGGAATGFIH
KQLKVGDAVE LSGPYGQFFV RDSQAGDLIF IAGGSGLSSP QSMILDLLER GDTRRITLFQ
GARNRAELYN CELFEELAAR HPNFSYVPAL NQANDDPEWQ GFKGFVHDAA KAHFDGRFGG
QKAYLCGPPP MIDAAITTLM QGRLFERDIF MERFYTAADG AGESSRSALF KRI
