ID A0A0B2C3X1_9SPHN Unreviewed; 390 AA.
AC A0A0B2C3X1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=4-hydroxybenzoate 3-monooxygenase {ECO:0000313|EMBL:KHL26691.1};
DE EC=1.14.13.2 {ECO:0000313|EMBL:KHL26691.1};
GN ORFNames=PK98_03095 {ECO:0000313|EMBL:KHL26691.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26691.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL26691.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL26691.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHL26691.1}.
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DR EMBL; JTDN01000001; KHL26691.1; -; Genomic_DNA.
DR RefSeq; WP_039096166.1; NZ_JTDN01000001.1.
DR AlphaFoldDB; A0A0B2C3X1; -.
DR STRING; 1572751.PK98_03095; -.
DR OrthoDB; 9791689at2; -.
DR Proteomes; UP000030988; Unassembled WGS sequence.
DR GO; GO:0018659; F:4-hydroxybenzoate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0043639; P:benzoate catabolic process; IEA:InterPro.
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; IPR012733; HB_mOase.
DR NCBIfam; TIGR02360; pbenz_hydroxyl; 1.
DR PANTHER; PTHR43476; 3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE; 1.
DR PANTHER; PTHR43476:SF4; BLR0106 PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:KHL26691.1};
KW Oxidoreductase {ECO:0000313|EMBL:KHL26691.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030988}.
FT DOMAIN 4..343
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 390 AA; 42596 MW; 179FBD9E5ABDF788 CRC64;
MRKQVCIVGA GPAGLLLGHL LRAEGIDCVV VEQRSPGYVL GRIRAGVLER ITVSLMEQLG
LDARLKAEGM PHGEFSLADG ERLIHIDLMD LVGQQVTVYG QTELTRDLME ACDARGLQVI
YGAEGVTLHD VATDAPFVTY TSSDGTEHRV EARFVVGCDG FHGPSRRAVP ASVGREYERV
YPFGWLGILA DVPPCGAGLI YANHERGFAL ASQRSPTRSR YYVDVPLTDR LEDWPDERIW
DELATRLGPE AAAHITRGPS IEKSIAPLRS YVFAPMRHGS LLLCGDSAHI VPPTGAKGLN
LAASDVYYAT EALRAFFGAN DPDAIGGYSD KALARVWKAE RFSWSLTRLM HRFPEDGPFE
RAMQVAELDY IASSRAAQTS IAENYVGLPV
//
