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P20586

- PHHY_PSEAE

UniProt

P20586 - PHHY_PSEAE

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Protein
p-hydroxybenzoate hydroxylase
Gene
pobA, PA0247
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FAD.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 3229FAD Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. 4-hydroxybenzoate 3-monooxygenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. benzoate catabolic process via hydroxylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00156; UER00257.

Names & Taxonomyi

Protein namesi
Recommended name:
p-hydroxybenzoate hydroxylase (EC:1.14.13.2)
Short name:
PHBH
Alternative name(s):
4-hydroxybenzoate 3-monooxygenase
Gene namesi
Name:pobA
Ordered Locus Names:PA0247
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA0247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394p-hydroxybenzoate hydroxylase
PRO_0000058381Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi208964.PA0247.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Helixi12 – 2413
Beta strandi28 – 314
Helixi36 – 405
Beta strandi47 – 493
Helixi50 – 589
Helixi63 – 686
Beta strandi70 – 734
Beta strandi75 – 795
Beta strandi82 – 865
Helixi88 – 925
Beta strandi97 – 993
Helixi102 – 11514
Beta strandi119 – 1235
Beta strandi125 – 1306
Beta strandi134 – 1363
Beta strandi138 – 1436
Beta strandi146 – 1516
Beta strandi153 – 1575
Helixi166 – 1683
Helixi171 – 1733
Beta strandi175 – 19218
Beta strandi195 – 1984
Beta strandi200 – 2023
Beta strandi209 – 2157
Beta strandi218 – 2258
Helixi231 – 2333
Helixi236 – 24510
Helixi249 – 2546
Beta strandi260 – 27415
Beta strandi276 – 2783
Beta strandi281 – 2833
Helixi285 – 2873
Helixi293 – 2953
Helixi298 – 31922
Helixi322 – 3276
Helixi328 – 35023
Helixi358 – 37316
Helixi375 – 38511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP20586.
SMRiP20586. Positions 1-394.

Miscellaneous databases

EvolutionaryTraceiP20586.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0654.
HOGENOMiHOG000221233.
KOiK00481.
OMAiLAEWSDA.
OrthoDBiEOG6PS5RW.
PhylomeDBiP20586.

Family and domain databases

InterProiIPR012733. HB_mOase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSiPR00420. RNGMNOXGNASE.
TIGRFAMsiTIGR02360. pbenz_hydroxyl. 1 hit.

Sequencei

Sequence statusi: Complete.

P20586-1 [UniParc]FASTAAdd to Basket

« Hide

MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ    50
GMVDLLREAG VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY 100
GQTEVTRDLM EAREACGATT VYQAAEVRLH DLQGERPYVT FERDGERLRL 150
DCDYIAGCDG FHGISRQSIP AERLKVFERV YPFGWLGLLA DTPPVSHELI 200
YANHPRGFAL CSQRSATRSR YYVQVPLSEK VEDWSDERFW TELKARLPSE 250
VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN 300
LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL 350
HRFPDTDAFS QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE 394
Length:394
Mass (Da):44,324
Last modified:February 1, 1991 - v1
Checksum:i1E7232854D9EC792
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23173 Genomic DNA. Translation: AAA88455.1.
AE004091 Genomic DNA. Translation: AAG03636.1.
PIRiJT0384. WHPSBA.
RefSeqiNP_248938.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG03636; AAG03636; PA0247.
GeneIDi882128.
KEGGipae:PA0247.
PATRICi19834710. VBIPseAer58763_0257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23173 Genomic DNA. Translation: AAA88455.1 .
AE004091 Genomic DNA. Translation: AAG03636.1 .
PIRi JT0384. WHPSBA.
RefSeqi NP_248938.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D7L X-ray 2.20 A 1-394 [» ]
1DOB X-ray 2.00 A 1-394 [» ]
1DOC X-ray 2.00 A 1-394 [» ]
1DOD X-ray 2.10 A 1-394 [» ]
1DOE X-ray 2.30 A 1-394 [» ]
1IUS X-ray 2.20 A 1-394 [» ]
1IUT X-ray 2.00 A 1-394 [» ]
1IUU X-ray 2.00 A 1-394 [» ]
1IUV X-ray 2.50 A 1-394 [» ]
1IUW X-ray 2.00 A 1-394 [» ]
1IUX X-ray 2.00 A 1-394 [» ]
1K0I X-ray 1.80 A 1-394 [» ]
1K0J X-ray 2.20 A 1-394 [» ]
1K0L X-ray 2.00 A 1-394 [» ]
1PXA X-ray 2.30 A 1-394 [» ]
1PXB X-ray 2.30 A 1-394 [» ]
1PXC X-ray 2.10 A 1-394 [» ]
1YKJ X-ray 2.00 A/B 1-394 [» ]
ProteinModelPortali P20586.
SMRi P20586. Positions 1-394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA0247.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG03636 ; AAG03636 ; PA0247 .
GeneIDi 882128.
KEGGi pae:PA0247.
PATRICi 19834710. VBIPseAer58763_0257.

Organism-specific databases

PseudoCAPi PA0247.

Phylogenomic databases

eggNOGi COG0654.
HOGENOMi HOG000221233.
KOi K00481.
OMAi LAEWSDA.
OrthoDBi EOG6PS5RW.
PhylomeDBi P20586.

Enzyme and pathway databases

UniPathwayi UPA00156 ; UER00257 .

Miscellaneous databases

EvolutionaryTracei P20586.

Family and domain databases

InterProi IPR012733. HB_mOase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view ]
Pfami PF01494. FAD_binding_3. 1 hit.
[Graphical view ]
PRINTSi PR00420. RNGMNOXGNASE.
TIGRFAMsi TIGR02360. pbenz_hydroxyl. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. 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.

Entry informationi

Entry nameiPHHY_PSEAE
AccessioniPrimary (citable) accession number: P20586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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