PHHY_ACIAD
ID PHHY_ACIAD Reviewed; 404 AA.
AC Q03298;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=p-hydroxybenzoate hydroxylase {ECO:0000250|UniProtKB:P20586};
DE Short=PHBH {ECO:0000250|UniProtKB:P20586};
DE EC=1.14.13.2 {ECO:0000250|UniProtKB:P20586};
DE AltName: Full=4-hydroxybenzoate 3-monooxygenase {ECO:0000250|UniProtKB:P20586};
GN Name=pobA; OrderedLocusNames=ACIAD1719;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8449410; DOI=10.1016/0378-1119(93)90741-k;
RA Dimarco A.A., Averhoff B.A., Kim E.E., Ornston L.N.;
RT "Evolutionary divergence of pobA, the structural gene encoding p-
RT hydroxybenzoate hydroxylase in an Acinetobacter calcoaceticus strain well-
RT suited for genetic analysis.";
RL Gene 125:25-33(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Catalyzes the incorporation of an atom of dioxygen into p-
CC hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The
CC reaction occurs in two parts: reduction of the flavin adenine
CC dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine
CC dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate
CC to the enzyme and oxidation of reduced FAD with oxygen to form a
CC hydroperoxide, which then oxygenates p-hydroxybenzoate.
CC {ECO:0000250|UniProtKB:P20586}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate
CC + H2O + NADP(+); Xref=Rhea:RHEA:19477, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.2; Evidence={ECO:0000250|UniProtKB:P20586};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P20586};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P20586};
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation; 3,4-dihydroxybenzoate from benzoate: step 2/2.
CC {ECO:0000250|UniProtKB:P20586}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P20586}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family.
CC {ECO:0000250|UniProtKB:P20586}.
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DR EMBL; L05770; AAC37163.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68561.1; -; Genomic_DNA.
DR RefSeq; WP_004926674.1; NC_005966.1.
DR AlphaFoldDB; Q03298; -.
DR SMR; Q03298; -.
DR STRING; 62977.ACIAD1719; -.
DR EnsemblBacteria; CAG68561; CAG68561; ACIAD1719.
DR GeneID; 45234106; -.
DR KEGG; aci:ACIAD1719; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_057691_0_0_6; -.
DR OMA; VVEPMQY; -.
DR OrthoDB; 1770293at2; -.
DR BioCyc; ASP62977:ACIAD_RS07925-MON; -.
DR UniPathway; UPA00156; UER00257.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0106356; F:4-hydroxybenzoate 3-monooxygenase [NADPH] activity; IEA:RHEA.
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:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012733; HB_mOase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02360; pbenz_hydroxyl; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..404
FT /note="p-hydroxybenzoate hydroxylase"
FT /id="PRO_0000058380"
FT BINDING 35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 45..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 301..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT SITE 203
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT SITE 387
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P20586"
SQ SEQUENCE 404 AA; 45271 MW; 43FC8E4266C07B3A CRC64;
MQTMKTKVAI IGSGPAGLLL GQLLYKAGIE HVIVEQRSAD YVASRIRAGI LEQVSVDLLE
QAGVDQNLKE KGLPHSGIEI LTNGQKFRVD LSALTQGKQV TVYGQTEVTK DLMQAREQAG
LCSFYESNDV QIHDFYNAPK VTFESNGTHY QIECDFIAGC DGYHGVCRAS VPQDKIKTFE
KVYPFGWLGV LADVPPVADE LIYVQSERGF ALCSMRSETR SRYYIQVPLT DHVENWSDDQ
FWEELKNRLD PESCEKLVTG PSIEKSIAPL RSFVTEPMRF GKLFLAGDAA HIVPPTGAKG
LNLAASDIAY LSSALIEFYT QGSEQGIDQY SEKCLQRVWK AERFSWWMTH LLHRFETESE
FDHKIKQAEL SYILGSTAGQ TTLAENYVGL PYEIKSLDYL KHAS
