ID A0A0U5MDA6_9PROT Unreviewed; 639 AA.
AC A0A0U5MDA6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative FAD-dependent Phenol 2-monooxygenase {ECO:0000313|EMBL:CUW37920.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:CUW37920.1};
GN ORFNames=XM1_0851 {ECO:0000313|EMBL:CUW37920.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW37920.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
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; LN997848; CUW37920.1; -; Genomic_DNA.
DR RefSeq; WP_068430049.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5MDA6; -.
DR STRING; 1663591.XM1_0851; -.
DR KEGG; magx:XM1_0851; -.
DR PATRIC; fig|1663591.3.peg.849; -.
DR OrthoDB; 9791689at2; -.
DR Proteomes; UP000063191; Chromosome I.
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:CUW37920.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CUW37920.1}.
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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 71308 MW; 16DAECB63AC8010E CRC64;
MQFHQDGFHP GDPRFADPQD RVVPPPIKRP LPAEVDVMIV GCGPAGLNLA AQLSKFPEIR
TCIADLKDDR LLVGQADGMA CRTLEMFQAY GFADQVIQEA YGVNEVTFWK PNPDAPAGIM
RNDRIQDVED DLSEMPHVII NQARIHDLFL DVMRQGPAKI EPFYSRKLVG LEVDRNAADH
PVTLTFERAV THSQTSKTLE TVRARYVVGC DGARSTVRQA IGRELVGDAL NQAWGVMDVL
VVTDFPDIRL KAVIHSANEG NMLIIPREGG YMVRLYIELD KLQENQRISR DSVTADYLIA
AARRIMRPYA IDVKEVAWWS VYEIGQRLTT AFDDSEPGRA PRVFLAGDAC HTHSPKAGQG
LNTSVNDTWN LGWKLAHVLK GRADADLLLS YSAERQDIAK QLIDFDRELA RMFSAKPKSA
DNPDGIDPAE FQRYFTQFGR FTAGTATHYK PSALVGDGAH QHLARGQILG MRFHSAPVIR
LADAKPMQLG HCIEADGRWR VFAFAGRAEP MGPDCGIRAL CEYLAGDSTS PLRRHTPEGA
DPDSVIDLRA VFQTPHRHMR LERLHPLLVP AKGRHGLKDY EKVFCPDFKS GRDIYDMRGI
DRDKGCVIVV RPDQYVAQVL PLADHDGLAR FFAGVLRAR
//
