ID A3VBL0_9RHOB Unreviewed; 639 AA.
AC A3VBL0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:EAQ14343.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:EAQ14343.1};
GN ORFNames=RB2654_16776 {ECO:0000313|EMBL:EAQ14343.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ14343.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ14343.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ14343.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ14343.1}.
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DR EMBL; AAMT01000002; EAQ14343.1; -; Genomic_DNA.
DR RefSeq; WP_008333706.1; NZ_VNHV01000004.1.
DR AlphaFoldDB; A3VBL0; -.
DR STRING; 314271.RB2654_16776; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_9_2_5; -.
DR OrthoDB; 9791689at2; -.
DR Proteomes; UP000002931; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
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:EAQ14343.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAQ14343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931}.
FT DOMAIN 34..405
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 441..605
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 71161 MW; 62D3A218B5A9EAEE CRC64;
MQYYEDGFRG GDPDLKKAAP GRRDRAPFAP LPDKVDVLIA GSGPAGTCLF AQLSQFPEID
TMLVERKPGP IEKGQADGIN TRTMEMFQAF GFGEKVKRES YWVNQTNFWV PDTANPGHIK
RIGRVQDVAD DSSEMPHTLI NQARVHELFL DVARKSAARN VPDYSWQVKD LTIDTTTEDH
PVTVILENTG INAGETHVVR ANYVVGCDGA RSSVRTAIGG KLEGDAAHQA WGVMDILANT
DFPDVRQKCL IASKSEGNVL ILPREGGYLF RMYVELDKLN PDERVSARNL TQDHMIAAAQ
RILTPYTLDV KEVVWWSVYE IGHRISETFD DVPPEDRATR NPRVFTAGDA CHTHSPKAGQ
GMNVSMQDTF NLGWKLAHVL TGRSDPSLLH TYRAERLTEA KRLVETDHKW ARIMSAPPGE
SELDGTDMPR IQKHFIENLE FTGGLAVKYD PSRVTGAATH QALATGEEIG RRFHSALVVR
VSDAMQMQLG HAAEADGRWR IYAFGGKEDT SEPGSALHKL ADWLESDPAS PIVRHTRKDE
GIDAVIDLRA IFQTTFDKMA YEKMPSLLKP IKGPLGLQDY EKVFCLDHKG LGDIYEMRGI
DRDKGCMIVV RPDQYVAHVL PLDGYDELSA FFADILLPV
//
