ID A0A161SUK6_9MICO Unreviewed; 611 AA.
AC A0A161SUK6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:KZE42843.1};
GN ORFNames=AVW09_08585 {ECO:0000313|EMBL:KZE42843.1};
OS Microbacterium sp. T32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1776083 {ECO:0000313|EMBL:KZE42843.1, ECO:0000313|Proteomes:UP000076494};
RN [1] {ECO:0000313|Proteomes:UP000076494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T32 {ECO:0000313|Proteomes:UP000076494};
RA Hong K.W.;
RT "Whole genome sequencing of Bhargavaea cecembensis T14.";
RL Submitted (JAN-2016) 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:KZE42843.1}.
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DR EMBL; LQQP01000004; KZE42843.1; -; Genomic_DNA.
DR RefSeq; WP_063256448.1; NZ_LQQP01000004.1.
DR AlphaFoldDB; A0A161SUK6; -.
DR STRING; 1776083.AVW09_08585; -.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000076494; Unassembled WGS sequence.
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:KZE42843.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076494}.
FT DOMAIN 32..389
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 420..572
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 66908 MW; 8FBA756061058F78 CRC64;
MQFHHHGYVS GDPRIQPAAG AGIDRPTELP DEVDVLIVGS GPAGMLLAAQ MSQFPQVTTR
LIEKRDGRLV LGQADGIQPR SVETFQAFGF ADRITAEAYN IGWMNFWAPD PDAPDRIVRT
TRTEDYALKI SEFPHLIVNQ ARVLDYFAEA AAHGPARIVP DYGVEFLGLT VGDDDVEVRV
RTIEGERTIR AKYLVGCDGA RSGVRHAIGR THVGAAAQHA WGVMDVLVET DFPDWRIKCA
ITAAAGAILH IPREGGYLSR MYIDLGEVAA DDDHRVRQTP IEEIIRRANR ILHPYSIDVK
QVAWHSVYEV GHCVTDQFVD DLHNPRVFLT GDACHTHSAK AGQGMNVSMQ DGFNLGWKLG
HVLTGLAPAE LLRTYDDERR PVAQQLIDFD REWSSLMARK PGEITDPDEL STYYLATAEF
PSGFMTQYGP SRIVAADAAQ DLASGFPIGK RFHSVEVVRV CDGNAVHLGH HAKADGRWRI
YAFADAGGSA LRAWADAARG IVERFTPADA DLDAVFDVKV VYPGRWEDVA DVPALFRPRS
GPLGLTDHEK VFAAAPSAWT SADIFAERGI GADGAVVVVR PDQYVAHVLP LSQPEALERF
LAGALRSPVP A
//
