ID PHHY_PSEAE Reviewed; 394 AA.
AC P20586;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 01-MAY-2013, entry version 100.
DE RecName: Full=p-hydroxybenzoate hydroxylase;
DE Short=PHBH;
DE EC=1.14.13.2;
DE AltName: Full=4-hydroxybenzoate 3-monooxygenase;
GN Name=pobA; OrderedLocusNames=PA0247;
OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS 12228).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2465205; DOI=10.1016/0378-1119(88)90044-3;
RA Entsch B., Nan Y., Weaich K., Scott K.F.;
RT "Sequence and organization of pobA, the gene coding for p-
RT hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas
RT aeruginosa.";
RL Gene 71:279-291(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT opportunistic pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7939628; DOI=10.1126/science.7939628;
RA Gatti D.L., Palfey B.A., Lah M.S., Entsch B., Massey V., Ballou D.P.,
RA Ludwig M.L.;
RT "The mobile flavin of 4-OH benzoate hydroxylase.";
RL Science 266:110-114(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8555229; DOI=10.1021/bi951344i;
RA Gatti D.L., Entsch B., Ballou D.P., Ludwig M.L.;
RT "pH-dependent structural changes in the active site of p-
RT hydroxybenzoate hydroxylase point to the importance of proton and
RT water movements during catalysis.";
RL Biochemistry 35:567-578(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS.
RX PubMed=8312276; DOI=10.1021/bi00172a036;
RA Lah M.S., Palfey B.A., Schreuder H.A., Ludwig M.L.;
RT "Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate
RT hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.";
RL Biochemistry 33:1555-1564(1994).
CC -!- CATALYTIC ACTIVITY: 4-hydroxybenzoate + NADPH + O(2) =
CC protocatechuate + NADP(+) + H(2)O.
CC -!- COFACTOR: FAD.
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation; 3,4-dihydroxybenzoate from benzoate: step 2/2.
CC -!- SUBUNIT: Homodimer.
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DR EMBL; M23173; AAA88455.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03636.1; -; Genomic_DNA.
DR PIR; JT0384; WHPSBA.
DR RefSeq; NP_248938.1; NC_002516.2.
DR PDB; 1D7L; X-ray; 2.20 A; A=1-394.
DR PDB; 1DOB; X-ray; 2.00 A; A=1-394.
DR PDB; 1DOC; X-ray; 2.00 A; A=1-394.
DR PDB; 1DOD; X-ray; 2.10 A; A=1-394.
DR PDB; 1DOE; X-ray; 2.30 A; A=1-394.
DR PDB; 1IUS; X-ray; 2.20 A; A=1-394.
DR PDB; 1IUT; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUU; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUV; X-ray; 2.50 A; A=1-394.
DR PDB; 1IUW; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUX; X-ray; 2.00 A; A=1-394.
DR PDB; 1K0I; X-ray; 1.80 A; A=1-394.
DR PDB; 1K0J; X-ray; 2.20 A; A=1-394.
DR PDB; 1K0L; X-ray; 2.00 A; A=1-394.
DR PDB; 1PXA; X-ray; 2.30 A; A=1-394.
DR PDB; 1PXB; X-ray; 2.30 A; A=1-394.
DR PDB; 1PXC; X-ray; 2.10 A; A=1-394.
DR PDB; 1YKJ; X-ray; 2.00 A; A/B=1-394.
DR PDBsum; 1D7L; -.
DR PDBsum; 1DOB; -.
DR PDBsum; 1DOC; -.
DR PDBsum; 1DOD; -.
DR PDBsum; 1DOE; -.
DR PDBsum; 1IUS; -.
DR PDBsum; 1IUT; -.
DR PDBsum; 1IUU; -.
DR PDBsum; 1IUV; -.
DR PDBsum; 1IUW; -.
DR PDBsum; 1IUX; -.
DR PDBsum; 1K0I; -.
DR PDBsum; 1K0J; -.
DR PDBsum; 1K0L; -.
DR PDBsum; 1PXA; -.
DR PDBsum; 1PXB; -.
DR PDBsum; 1PXC; -.
DR PDBsum; 1YKJ; -.
DR ProteinModelPortal; P20586; -.
DR SMR; P20586; 1-394.
DR STRING; 208964.PA0247; -.
DR GeneID; 882128; -.
DR KEGG; pae:PA0247; -.
DR PATRIC; 19834710; VBIPseAer58763_0257.
DR PseudoCAP; PA0247; -.
DR eggNOG; COG0654; -.
DR HOGENOM; HOG000221233; -.
DR KO; K00481; -.
DR OMA; WSDERFW; -.
DR ProtClustDB; PRK08243; -.
DR UniPathway; UPA00156; UER00257.
DR EvolutionaryTrace; P20586; -.
DR GO; GO:0018659; F:4-hydroxybenzoate 3-monooxygenase activity; IEA:EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR012733; HB_mOase.
DR InterPro; IPR002938; mOase_FAD-bd.
DR InterPro; IPR003042; Rng_hydrolase-like.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR TIGRFAMs; TIGR02360; pbenz_hydroxyl; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1 394 p-hydroxybenzoate hydroxylase.
FT /FTId=PRO_0000058381.
FT NP_BIND 4 32 FAD (Potential).
FT STRAND 4 8
FT HELIX 12 24
FT STRAND 28 31
FT HELIX 36 40
FT STRAND 47 49
FT HELIX 50 58
FT HELIX 63 68
FT STRAND 70 73
FT STRAND 75 79
FT STRAND 82 86
FT HELIX 88 92
FT STRAND 97 99
FT HELIX 102 115
FT STRAND 119 123
FT STRAND 125 130
FT STRAND 134 136
FT STRAND 138 143
FT STRAND 146 151
FT STRAND 153 157
FT HELIX 166 168
FT HELIX 171 173
FT STRAND 175 192
FT STRAND 195 198
FT STRAND 200 202
FT STRAND 209 215
FT STRAND 218 225
FT HELIX 231 233
FT HELIX 236 245
FT HELIX 249 254
FT STRAND 260 274
FT STRAND 276 278
FT STRAND 281 283
FT HELIX 285 287
FT HELIX 293 295
FT HELIX 298 319
FT HELIX 322 327
FT HELIX 328 350
FT HELIX 358 373
FT HELIX 375 385
SQ SEQUENCE 394 AA; 44324 MW; 1E7232854D9EC792 CRC64;
MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ GMVDLLREAG
VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY GQTEVTRDLM EAREACGATT
VYQAAEVRLH DLQGERPYVT FERDGERLRL DCDYIAGCDG FHGISRQSIP AERLKVFERV
YPFGWLGLLA DTPPVSHELI YANHPRGFAL CSQRSATRSR YYVQVPLSEK VEDWSDERFW
TELKARLPSE VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN
LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL HRFPDTDAFS
QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE
//
