ID D6BK78_9GAMM Unreviewed; 353 AA.
AC D6BK78;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Phenol hydroxylase protein {ECO:0000313|EMBL:ACL31147.1};
GN Name=mphP {ECO:0000313|EMBL:ACL31147.1};
OS Acinetobacter sp. MO.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=398699 {ECO:0000313|EMBL:ACL31147.1};
RN [1] {ECO:0000313|EMBL:ACL31147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MO {ECO:0000313|EMBL:ACL31147.1};
RA Davolos D., Pietrangeli B.;
RT "Molecular and phylogenetic analysis on bacteria isolated from wastewater
RT samples of an Italian steel industry.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EU938358; ACL31147.1; -; Genomic_DNA.
DR AlphaFoldDB; D6BK78; -.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06211; phenol_2-monooxygenase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..201
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 353 AA; 39014 MW; B9BE6BA14C9ADFFD CRC64;
MSYQVTIEPI GTTIEVEEDQ TILDAALRQG VWLPFACGHG TCGTCKVQVT DGYYDVGEAS
PFALMDLERE EHKVLACCCK PESDMTIEAD VDEDPDFLGY LVQDYQAKVL EVKDLSPTIK
GVRLQLDRPM EFQAGQYINV QFPGIEGTRA FSIANAPSEL GIIELHIRHV VGGSATTYVH
EQLAAGDALE ISGPYGQFFV RKSDDQDAIF IAGGSGLSSP QSMILDLLES GDTRTIYLFQ
GARDVAELYN RELFEQLVKD YPNFRYIPAL NAPKAEDHWT GFTGYVHEAV ADYFEQRCGG
HKAYLCGPPV MIDAAISTLM QSRLFERDIH TERFLSAADG ASGQSRSALF KHI
//
