ID A0A097IF26_9CORY Unreviewed; 395 AA.
AC A0A097IF26;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:AIT60731.1};
GN ORFNames=CDOO_05295 {ECO:0000313|EMBL:AIT60731.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT60731.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT60731.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT60731.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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; CP006764; AIT60731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097IF26; -.
DR STRING; 558173.CDOO_05295; -.
DR KEGG; cdo:CDOO_05295; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_9_0_11; -.
DR Proteomes; UP000029914; 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:AIT60731.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029914}.
FT DOMAIN 1..171
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 202..361
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 395 AA; 44085 MW; ADBFE830F0F50C4C CRC64;
MDMVVDTDFP DWRTKCSIHS KAGSILHIPR EGGFLCRIYV DLGQVLEDDN GRIRETPVKK
VIAKANEIYH PYSIDVKDVA WSSVYEVGHR LVDAFDNSNP DNPDHHPHVF LTGDACHTHS
AKAGQGMNVS MQDGFNIGWK LGAVLSGQAS EKLLLTYHGE RQPAAQNLIN FDKQWSTLMA
TPPELLEDPQ AVEKFYVSAE EFAAGMLTTY EQNLIVGDTT HQDLATGFPV GRRFKSHKAM
RRCDAVVTHI GHEHVADGRW RIYAFADSPA PGEPSKMTAW ADWMKTDDAS PLRRFTPAEG
DDNAVFDIKG IYRQGHHDFE LFDAPDVFFP RMGTLSLTSY ENVYAALPGE DIFAGRGISR
DGAVVVVRPD QYVAAVLPLE DTAGLSEFFD RFLRE
//
