ID A0A0Q9R0Z4_9MICC Unreviewed; 630 AA.
AC A0A0Q9R0Z4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:KRF08863.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:KRF08863.1};
GN ORFNames=ASH00_04050 {ECO:0000313|EMBL:KRF08863.1};
OS Arthrobacter sp. Soil782.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF08863.1, ECO:0000313|Proteomes:UP000053496};
RN [1] {ECO:0000313|EMBL:KRF08863.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF08863.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF08863.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF08863.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KRF08863.1}.
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DR EMBL; LMSO01000001; KRF08863.1; -; Genomic_DNA.
DR RefSeq; WP_056545269.1; NZ_LMSO01000001.1.
DR AlphaFoldDB; A0A0Q9R0Z4; -.
DR STRING; 1736410.ASH00_04050; -.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000053496; 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:KRF08863.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KRF08863.1}.
FT DOMAIN 32..404
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 435..592
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 630 AA; 69382 MW; 18FFAB67807CC2C9 CRC64;
MHFHHHGYVS GDPRVQAAAG VGVNRSEELP EEVDVLIVGS GPAGMLAAAQ LSQFPNITTR
LVERRPGRLA IGQADGIQAR SVETFQAFGF AERITAEAYR ITEMAFWKPD PADPSRIIRT
ARPLDDPTGI SEFPHLIVNQ ARVLDYFAEF MANAPTRMTP DYGLDFQSLE VDEGGEYPVT
VTLLHTAGPR EGQERTVRAK YVIGADGARS KVRQAIGCTL AGDAANHAWG VMDVLAVTDF
PDIRLKCAIQ SGTGGSILLI PREGGHLFRM YVDLGEVDAH TKGDIRSTTI EEVIEKANAI
LYPYTLDVRN VAWNSVYEVG HRLTDRFDDV LPEDIGTRTP RVFITGDACH THSAKAGQGM
NVSMQDGFNI AWKLGHVLEG RSKESLLSTY SAERQVVAKN LIDFDKQWSS LMAKKPEEFE
DPTELENFYV RTMEFPAGFM TEYSPSMIVA EAVHQELATG FPVGKRFKSA PVVRVCDTNP
LHLGHHATAD GRWRIYVFAD EPLPGNPSKV TNFAEWLTNS PESPLAATPE GADLDAWFDV
KVIYQQDHQS IDINAVPAVF KPEVGPFKLN YLEKVFGTDQ AEDIFELRGL DRGGVVVVVR
PDQYVANVLP LTATAELGEF FAGMRAGVPR
//
