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Protein

p-hydroxybenzoate hydroxylase

Gene

pobA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.7 Publications

Catalytic activityi

4-hydroxybenzoate + NADPH + O2 = protocatechuate + NADP+ + H2O.1 Publication

Cofactori

FAD6 PublicationsNote: Binds 1 FAD per subunit.5 Publications

Pathwayi: benzoate degradation via hydroxylation

This protein is involved in step 2 of the subpathway that synthesizes 3,4-dihydroxybenzoate from benzoate.Curated
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. p-hydroxybenzoate hydroxylase (pobA)
This subpathway is part of the pathway benzoate degradation via hydroxylation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3,4-dihydroxybenzoate from benzoate, the pathway benzoate degradation via hydroxylation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13FAD6 Publications1
Binding sitei32FAD6 Publications1
Binding sitei102FAD6 Publications1
Binding sitei201Substrate6 Publications1
Sitei201Important for catalytic activity1 Publication1
Binding sitei222Substrate6 Publications1
Binding sitei286FAD5 Publications1
Binding sitei293Substrate; via carbonyl oxygen6 Publications1
Sitei385Important for catalytic activity1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 47FAD6 Publications6
Nucleotide bindingi299 – 300FAD6 Publications2

GO - Molecular functioni

  • 4-hydroxybenzoate 3-monooxygenase activity Source: UniProtKB
  • FAD binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.2. 5087.
UniPathwayiUPA00156; UER00257.

Names & Taxonomyi

Protein namesi
Recommended name:
p-hydroxybenzoate hydroxylase1 Publication (EC:1.14.13.21 Publication)
Short name:
PHBH1 Publication
Alternative name(s):
4-hydroxybenzoate 3-monooxygenaseCurated
Gene namesi
Name:pobA1 Publication
Ordered Locus Names:PA0247
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0247.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45A → G: The positions of the substrate and the flavin are not altered. 1 Publication1
Mutagenesisi201Y → F: Reduction of hydroxylase activity. 2 Publications1
Mutagenesisi220R → Q: Lower affinity for p-OHB than the wild-type. 1 Publication1
Mutagenesisi300N → D: The side chain of Asp300 moves away from the flavin, disrupting the interactions of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interactions with the flavin ring. 1 Publication1
Mutagenesisi385Y → F: The positions of the substrate and the flavin are not altered. 2 Publications1

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000583811 – 394p-hydroxybenzoate hydroxylaseAdd BLAST394

Proteomic databases

PaxDbiP20586.

Interactioni

Subunit structurei

Homodimer.6 Publications

Protein-protein interaction databases

STRINGi208964.PA0247.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi12 – 24Combined sources13
Beta strandi28 – 31Combined sources4
Helixi36 – 40Combined sources5
Beta strandi47 – 49Combined sources3
Helixi50 – 58Combined sources9
Helixi63 – 68Combined sources6
Beta strandi70 – 73Combined sources4
Beta strandi75 – 79Combined sources5
Beta strandi82 – 86Combined sources5
Helixi88 – 92Combined sources5
Beta strandi97 – 99Combined sources3
Helixi102 – 115Combined sources14
Beta strandi119 – 123Combined sources5
Beta strandi125 – 130Combined sources6
Beta strandi134 – 136Combined sources3
Beta strandi138 – 143Combined sources6
Beta strandi146 – 151Combined sources6
Beta strandi153 – 157Combined sources5
Helixi166 – 168Combined sources3
Helixi171 – 173Combined sources3
Beta strandi175 – 192Combined sources18
Beta strandi195 – 198Combined sources4
Beta strandi200 – 202Combined sources3
Beta strandi209 – 215Combined sources7
Beta strandi218 – 225Combined sources8
Helixi231 – 233Combined sources3
Helixi236 – 245Combined sources10
Helixi249 – 254Combined sources6
Beta strandi260 – 274Combined sources15
Beta strandi276 – 278Combined sources3
Beta strandi281 – 283Combined sources3
Helixi285 – 287Combined sources3
Helixi293 – 295Combined sources3
Helixi298 – 319Combined sources22
Helixi322 – 327Combined sources6
Helixi328 – 350Combined sources23
Helixi358 – 373Combined sources16
Helixi375 – 385Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20586.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 214Substrate binding6 Publications3

Sequence similaritiesi

Belongs to the aromatic-ring hydroxylase family.Curated

Phylogenomic databases

eggNOGiENOG41072AC. Bacteria.
COG0654. LUCA.
HOGENOMiHOG000221233.
InParanoidiP20586.
KOiK00481.
OMAiVWKGERF.
PhylomeDBiP20586.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR012733. HB_mOase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
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.
WP_003112685.1. NZ_ASJY01000056.1.

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.
PIRiJT0384. WHPSBA.
RefSeqiNP_248938.1. NC_002516.2.
WP_003112685.1. NZ_ASJY01000056.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi208964.PA0247.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP20586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

PseudoCAPiPA0247.

Phylogenomic databases

eggNOGiENOG41072AC. Bacteria.
COG0654. LUCA.
HOGENOMiHOG000221233.
InParanoidiP20586.
KOiK00481.
OMAiVWKGERF.
PhylomeDBiP20586.

Enzyme and pathway databases

UniPathwayiUPA00156; UER00257.
BRENDAi1.14.13.2. 5087.

Miscellaneous databases

EvolutionaryTraceiP20586.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR012733. HB_mOase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR02360. pbenz_hydroxyl. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Controlled catalysis is achieved by movement of the flavin and protein between three conformations: in, out and open. The open conformation is important for substrate binding and product release, the in conformation for reaction with oxygen and hydroxylation, and the out conformation for the reduction of FAD by NADPH.1 Publication

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
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.