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P00438 (PHHY_PSEFL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
p-hydroxybenzoate hydroxylase

EC=1.14.13.2
Alternative name(s):
4-hydroxybenzoate 3-monooxygenase
Gene names
Name:pobA
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

4-hydroxybenzoate + NADPH + O2 = protocatechuate + NADP+ + H2O.

Cofactor

FAD.

Pathway

Aromatic compound metabolism; benzoate degradation via hydroxylation; 3,4-dihydroxybenzoate from benzoate: step 2/2.

Subunit structure

Homodimer.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394p-hydroxybenzoate hydroxylase
PRO_0000058382

Regions

Nucleotide binding4 – 3330FAD Potential
Nucleotide binding276 – 28611FAD Potential

Experimental info

Sequence conflict3441W → Y AA sequence Ref.2

Secondary structure

........................................................................ 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00438 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: D29599224AC81E00

FASTA39444,322
        10         20         30         40         50         60 
MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ GMVDLLREAG 

        70         80         90        100        110        120 
VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY GQTEVTRDLM EAREACGATT 

       130        140        150        160        170        180 
VYQAAEVRLH DLQGERPYVT FERDGERLRL DCDYIAGCDG FHGISRQSIP AERLKVFERV 

       190        200        210        220        230        240 
YPFGWLGLLA DTPPVSHELI YANHPRGFAL CSQRSATRSR YYVQVPLTEK VEDWSDERFW 

       250        260        270        280        290        300 
TELKARLPAE VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN 

       310        320        330        340        350        360 
LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL HRFPDTDAFS 

       370        380        390 
QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE 

« Hide

References

[1]"Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens."
van Berkel W., Westphal A., Eschrich K., Eppink M., de Kok A.
Eur. J. Biochem. 210:411-419(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens."
Weijer W.J., Hofsteenge J., Vereijken J.M., Jekel P.A., Beintema J.J.
Biochim. Biophys. Acta 704:385-388(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide."
Hofsteenge J., Vereijken J.M., Weijer W.J., Beintema J.J., Wierenga R.K., Drenth J.
Eur. J. Biochem. 113:141-150(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 111-138 AND 270-280.
[4]"The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens."
Vereijken J.M., Hofsteenge J., Bak H.J., Beintema J.J.
Eur. J. Biochem. 113:151-157(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-52; 53-65 AND 66-110.
[5]"p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure."
Hofsteenge J., Weijer W.J., Jekel P.A., Beintema J.J.
Eur. J. Biochem. 133:91-108(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF CNBR PEPTIDES AND TERTIARY STRUCTURE.
[6]"p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure."
Weijer W.J., Hofsteenge J., Beintema J.J., Wierenga R.K., Drenth J.
Eur. J. Biochem. 133:109-118(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF CNBR PEPTIDES, FAD BINDING SITE.
[7]"Crystal structure of p-hydroxybenzoate hydroxylase."
Wierenga R.K., de Jong R.J., Kalk K.H., Hol W.G.J., Drenth J.
J. Mol. Biol. 131:55-73(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[8]"Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate."
Schreuder H.A., van der Laan J.M., Hol W.G.J., Drenth J.
J. Mol. Biol. 199:637-648(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]"Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3-A resolution."
Schreuder H.A., van der Laan J.M., Swarte M.B.A., Kalk K.H., Hol W.G.J., Drenth J.
Proteins 14:178-190(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM.
[10]"Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding."
Eppink M.H., Schreuder H.A., van Berkel W.J.
Eur. J. Biochem. 231:157-165(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44.
[11]"Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding."
Eppink M.H., Schreuder H.A., van Berkel W.J.
Eur. J. Biochem. 253:194-201(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42.
[12]"Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability."
Eppink M.H., Bunthol C., Schreuder H.A., van Berkel W.J.
FEBS Lett. 443:251-255(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68438 Genomic DNA. Translation: CAA48483.1.
PIRWHPSBF. A90643.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF3X-ray2.20A1-394[»]
1BGJX-ray3.00A1-394[»]
1BGNX-ray2.00A1-394[»]
1BKWX-ray2.20A1-394[»]
1CC4X-ray2.00A1-394[»]
1CC6X-ray2.20A1-394[»]
1CJ2X-ray2.80A1-391[»]
1CJ3X-ray2.50A1-392[»]
1CJ4X-ray2.40A1-392[»]
1PBBX-ray2.50A1-394[»]
1PBCX-ray2.80A1-394[»]
1PBDX-ray2.30A1-394[»]
1PBEX-ray1.90A1-394[»]
1PBFX-ray2.70A1-394[»]
1PDHX-ray2.10A1-394[»]
1PHHX-ray2.30A1-394[»]
2PHHX-ray2.70A1-394[»]
ProteinModelPortalP00438.
SMRP00438. Positions 1-394.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11534.
UniPathwayUPA00156; UER00257.

Family and domain databases

InterProIPR012733. HB_mOase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
TIGRFAMsTIGR02360. pbenz_hydroxyl. 1 hit.
ProtoNetSearch...

Other

BindingDBP00438.
ChEMBLCHEMBL3675.
DrugBankDB00233. Aminosalicylic Acid.
EvolutionaryTraceP00438.

Entry information

Entry namePHHY_PSEFL
AccessionPrimary (citable) accession number: P00438
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references