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Database: UniProt
Entry: Q2G5K1_NOVAD
LinkDB: Q2G5K1_NOVAD
Original site: Q2G5K1_NOVAD 
ID   Q2G5K1_NOVAD            Unreviewed;       389 AA.
AC   Q2G5K1;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=4-hydroxybenzoate 3-monooxygenase {ECO:0000313|EMBL:ABD26872.1};
DE            EC=1.14.13.2 {ECO:0000313|EMBL:ABD26872.1};
GN   OrderedLocusNames=Saro_2436 {ECO:0000313|EMBL:ABD26872.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26872.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000248; ABD26872.1; -; Genomic_DNA.
DR   RefSeq; WP_011446078.1; NC_007794.1.
DR   AlphaFoldDB; Q2G5K1; -.
DR   STRING; 279238.Saro_2436; -.
DR   KEGG; nar:Saro_2436; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_057691_0_0_5; -.
DR   Proteomes; UP000009134; Chromosome.
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:ABD26872.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABD26872.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT   DOMAIN          2..342
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   389 AA;  42745 MW;  977F337B09C5300E CRC64;
     MKTQVAIIGA GPAGLLLGHL LKAEGIDCVV LERQTPDYVL GRIRAGVLEQ ITVGLMERLG
     LDARLKAEGL VEEGFNLADG ERLIRIDVAN LTGKTVVVYG QTEITKDLMD AAPERGLQVI
     YGASEVALFD IESDAPYVTY VHDGAPRRID ARFIVGCDGF HGPSRKAIPA SVAREYERVY
     PFGWLGILAD VPPCNHELIY ANHERGFALA SMRSHTRSRY YVDVPLTEKV EDWSDERIWD
     ELAVRLGPEA AANITRGPSI EKSIAPLRSY VFEPMRHGSL LLCGDAAHIV PPTGAKGLNL
     AASDVHYAAE ALTGFFKRAD NDAVPRYSAK ALARVWKSER FSWSLTKLMH RFPEDGPFER
     AMQVAELEYI ATSKAAQTSI AENYVGLPV
//
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