Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20586

- PHHY_PSEAE

UniProt

P20586 - PHHY_PSEAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

p-hydroxybenzoate hydroxylase

Gene

pobA

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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 3229FADSequence AnalysisAdd
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.

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394p-hydroxybenzoate hydroxylasePRO_0000058381Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi208964.PA0247.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi12 – 2413Combined sources
Beta strandi28 – 314Combined sources
Helixi36 – 405Combined sources
Beta strandi47 – 493Combined sources
Helixi50 – 589Combined sources
Helixi63 – 686Combined sources
Beta strandi70 – 734Combined sources
Beta strandi75 – 795Combined sources
Beta strandi82 – 865Combined sources
Helixi88 – 925Combined sources
Beta strandi97 – 993Combined sources
Helixi102 – 11514Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi153 – 1575Combined sources
Helixi166 – 1683Combined sources
Helixi171 – 1733Combined sources
Beta strandi175 – 19218Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi209 – 2157Combined sources
Beta strandi218 – 2258Combined sources
Helixi231 – 2333Combined sources
Helixi236 – 24510Combined sources
Helixi249 – 2546Combined sources
Beta strandi260 – 27415Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi281 – 2833Combined sources
Helixi285 – 2873Combined sources
Helixi293 – 2953Combined sources
Helixi298 – 31922Combined sources
Helixi322 – 3276Combined sources
Helixi328 – 35023Combined sources
Helixi358 – 37316Combined sources
Helixi375 – 38511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20586.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0654.
HOGENOMiHOG000221233.
InParanoidiP20586.
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

        10         20         30         40         50
MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ
60 70 80 90 100
GMVDLLREAG VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY
110 120 130 140 150
GQTEVTRDLM EAREACGATT VYQAAEVRLH DLQGERPYVT FERDGERLRL
160 170 180 190 200
DCDYIAGCDG FHGISRQSIP AERLKVFERV YPFGWLGLLA DTPPVSHELI
210 220 230 240 250
YANHPRGFAL CSQRSATRSR YYVQVPLSEK VEDWSDERFW TELKARLPSE
260 270 280 290 300
VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN
310 320 330 340 350
LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL
360 370 380 390
HRFPDTDAFS QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE
Length:394
Mass (Da):44,324
Last modified:February 1, 1991 - v1
Checksum:i1E7232854D9EC792
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

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.
InParanoidi P20586.
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: November 26, 2014
This is version 110 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