ID A0A0U3QKF3_9MICC Unreviewed; 630 AA.
AC A0A0U3QKF3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:ALV47150.1};
GN ORFNames=MB46_18300 {ECO:0000313|EMBL:ALV47150.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV47150.1, ECO:0000313|Proteomes:UP000055883};
RN [1] {ECO:0000313|EMBL:ALV47150.1, ECO:0000313|Proteomes:UP000055883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:ALV47150.1,
RC ECO:0000313|Proteomes:UP000055883};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; CP013745; ALV47150.1; -; Genomic_DNA.
DR RefSeq; WP_044579290.1; NZ_CP013745.1.
DR AlphaFoldDB; A0A0U3QKF3; -.
DR KEGG; arw:MB46_18300; -.
DR eggNOG; COG0654; Bacteria.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000055883; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:ALV47150.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 33..404
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 435..594
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 69406 MW; 0989202933611FBA CRC64;
MQFHQHGYVS GDPRIKPAAG TGVDRPAQLP ELMDVLIVGS GPAGMITAAQ LSAFPNINTR
IVERRGGRLE IGQADGIQAR SVETFQAFGF AERIIAEAYR ITATVFWKPD PADHSKIVRA
ARAPDDTTGI SEFPHLIVNQ ARVLDYFAEV MAYSPSRMKP DYGWEFRSLS IDESGDYPVA
VTLVGTQGEL AGVERVVHAK YVVGADGAHS AVRESIGARH TSVHANHAWG VMDVLAVTDF
PDIRSKCAIQ SEDGGNILLI PREGGSLFRM YVDLGEVVAG GDRSVRGTTI DEIIAKANKI
LHPYTLDVKS VAWNSVYEVG HRLTDRFDDV PLDQLDDRLP RVFITGDACH THSAKAGQGM
NVSMQDGFNL AWKIAHVVEG RSPASLLATY SAERKVIAKN LIDFDLQWSS LMAKRPEDGG
DSTELEDFYV RTFEFPAGFM TQYQPSMIVA EATHQELATG FPVGKRFKSA PVVRVADVNP
VQLGHHHRAD GRWRLYAFAD SPAVGEPSAL LEWARWLSTS DDSPLLKYTP EDDDIDAVFD
VLLIAQQDFE GVDLRRVPVT FMPRTGPFGL IDYELVYAAD PDRDIFQARG ISRDGAVVVV
RPDQYVANVL PLQATTELAD FFARTMQPRR
//
