DMPP_ACICP
ID DMPP_ACICP Reviewed; 353 AA.
AC Q7WTJ2; F0KIB8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phenol hydroxylase P5 protein;
DE EC=1.14.13.7;
DE AltName: Full=Phenol 2-monooxygenase P5 component;
GN Name=mphP; OrderedLocusNames=BDGL_000470;
OS Acinetobacter calcoaceticus (strain PHEA-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=871585;
RN [1] {ECO:0000312|EMBL:CAD92316.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PHEA-2 {ECO:0000312|EMBL:CAD92316.1};
RX PubMed=12732969; DOI=10.1007/s00284-002-3840-4;
RA Xu Y., Chen M., Zhang W., Lin M.;
RT "Genetic organization of genes encoding phenol hydroxylase, benzoate 1,2-
RT dioxygenase alpha subunit and its regulatory proteins in Acinetobacter
RT calcoaceticus PHEA-2.";
RL Curr. Microbiol. 46:235-240(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHEA-2;
RX PubMed=21441526; DOI=10.1128/jb.00261-11;
RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA Yuan M., Zhou Z., Elmerich C., Lin M.;
RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT industry wastewater.";
RL J. Bacteriol. 193:2672-2673(2011).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-26, AND INDUCTION.
RC STRAIN=69-V;
RA Benndorf D., Loffhagen N., Hartig C., Babel W.;
RT "Growth on phenol at chemostress levels amplifies the expression of the
RT phenol degradation pathway in Acinetobacter calcoaceticus.";
RL Eng. Life Sci. 4:38-42(2004).
CC -!- FUNCTION: Catabolizes phenol, and some of its methylated derivatives.
CC P5 is required for growth on phenol, and for in vitro phenol
CC hydroxylase activity (By similarity). {ECO:0000250|UniProtKB:P19734}.
CC -!- FUNCTION: Probable electron transfer from NADPH, via FAD and the 2Fe-2S
CC center, to the oxygenase activity site of the enzyme.
CC {ECO:0000250|UniProtKB:P19734}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+);
CC Xref=Rhea:RHEA:17061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:18135,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.7;
CC Evidence={ECO:0000250|UniProtKB:P19734};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC -!- SUBUNIT: The multicomponent enzyme phenol hydroxylase is formed by P0,
CC P1, P2, P3, P4 and P5 polypeptides. {ECO:0000250|UniProtKB:P19734}.
CC -!- INDUCTION: By phenol. {ECO:0000269|Ref.3, ECO:0000305}.
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; AJ564846; CAD92316.1; -; Genomic_DNA.
DR EMBL; CP002177; ADY81056.1; -; Genomic_DNA.
DR RefSeq; WP_014206216.1; NC_016603.1.
DR RefSeq; YP_004994738.1; NC_016603.1.
DR AlphaFoldDB; Q7WTJ2; -.
DR SMR; Q7WTJ2; -.
DR STRING; 871585.BDGL_000470; -.
DR TCDB; 5.B.1.3.2; the phagocyte (gp91(phox)) nadph oxidase family.
DR EnsemblBacteria; ADY81056; ADY81056; BDGL_000470.
DR GeneID; 11638648; -.
DR KEGG; acc:BDGL_000470; -.
DR PATRIC; fig|871585.3.peg.467; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR OMA; KKWQCEV; -.
DR UniPathway; UPA00728; -.
DR Proteomes; UP000007477; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0046191; P:aerobic phenol-containing compound catabolic process; ISS: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; NADP; Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..353
FT /note="Phenol hydroxylase P5 protein"
FT /id="PRO_0000189406"
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; 39038 MW; CFA97CFD40458549 CRC64;
MSYQVTIEPI GTTIEVEEDQ TILDAALRQG VWLPFACGHG TCGTCKVQVT DGFYDVGEAS
PFALMDIERD ENKVLACCCK PQSDMVIEAD VDEDPDFLGH LVQDYQATVI EIKDLSPTIK
GIRLQLDRPI EFQAGQYINV QFPNIEGTRA FSIANSPSEV GIVELHIRKV EGGAATTYVH
EQLATGDQLD ISGPYGQFFV RKSDDQNAIF IAGGSGLSSP QSMILDLLES GDSRTIYLFQ
GARDLAELYN RELFEQLVKD YPNFRYIPAL NAPKPEDQWT GFTGFVHEAV ADYFENRCGG
HKAYLCGPPI MIDSAISTLM QSRLFERDIH TERFLSAADG AAGQSRSALF KHI
