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P20586 (PHHY_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Short name=PHBH
EC=1.14.13.2
Alternative name(s):
4-hydroxybenzoate 3-monooxygenase
Gene names
Name:pobA
Ordered Locus Names:PA0247
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [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_0000058381

Regions

Nucleotide binding4 – 3229FAD Potential

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P20586 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 1E7232854D9EC792

FASTA39444,324
        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 YYVQVPLSEK VEDWSDERFW 

       250        260        270        280        290        300 
TELKARLPSE 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

« Hide 'large scale' references
[1]"Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa."
Entsch B., Nan Y., Weaich K., Scott K.F.
Gene 71:279-291(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"The mobile flavin of 4-OH benzoate hydroxylase."
Gatti D.L., Palfey B.A., Lah M.S., Entsch B., Massey V., Ballou D.P., Ludwig M.L.
Science 266:110-114(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]"pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis."
Gatti D.L., Entsch B., Ballou D.P., Ludwig M.L.
Biochemistry 35:567-578(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants."
Lah M.S., Palfey B.A., Schreuder H.A., Ludwig M.L.
Biochemistry 33:1555-1564(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23173 Genomic DNA. Translation: AAA88455.1.
AE004091 Genomic DNA. Translation: AAG03636.1.
PIRWHPSBA. JT0384.
RefSeqNP_248938.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7LX-ray2.20A1-394[»]
1DOBX-ray2.00A1-394[»]
1DOCX-ray2.00A1-394[»]
1DODX-ray2.10A1-394[»]
1DOEX-ray2.30A1-394[»]
1IUSX-ray2.20A1-394[»]
1IUTX-ray2.00A1-394[»]
1IUUX-ray2.00A1-394[»]
1IUVX-ray2.50A1-394[»]
1IUWX-ray2.00A1-394[»]
1IUXX-ray2.00A1-394[»]
1K0IX-ray1.80A1-394[»]
1K0JX-ray2.20A1-394[»]
1K0LX-ray2.00A1-394[»]
1PXAX-ray2.30A1-394[»]
1PXBX-ray2.30A1-394[»]
1PXCX-ray2.10A1-394[»]
1YKJX-ray2.00A/B1-394[»]
ProteinModelPortalP20586.
SMRP20586. Positions 1-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882128.
KEGGpae:PA0247.
PATRIC19834710. VBIPseAer58763_0257.

Organism-specific databases

PseudoCAPPA0247.

Phylogenomic databases

eggNOGCOG0654.
HOGENOMHOG000221233.
KOK00481.
OMAVEPMQYG.
OrthoDBEOG6PS5RW.
ProtClustDBPRK08243.

Enzyme and pathway databases

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

EvolutionaryTraceP20586.

Entry information

Entry namePHHY_PSEAE
AccessionPrimary (citable) accession number: P20586
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways