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Protein

Isochorismate pyruvate lyase

Gene

pchB

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

Involved in the incorporation of salicylate into the siderophore pyochelin. Catalyzes the elimination of the enolpyruvyl side chain from isochorismate to yield salicylate and pyruvate via a rare pericyclic hydrogen transfer mechanism from C2 to C5. PchB also catalyzes the nonphysiological Claisen rearrangement of chorismate to prephenate in which the pyruvylenol tail is transferred from a C3 ether linkage to a C1-C9 linkage.6 Publications

Catalytic activityi

Isochorismate = salicylate + pyruvate.4 Publications
Chorismate = prephenate.3 Publications

Enzyme regulationi

Inhibited by endo-oxabicyclic diacid resembling to the conformation of the transition state.1 Publication

Kineticsi

Kcat is 1.01 sec(-1) for lyase activity (at pH 7.5 and 22 degrees Celsius). Kcat is 23.5 sec(-1) for chorismate mutase activity (at pH 7.5 and 22 degrees Celsius). Kcat is 106 min(-1) for lyase activity (at pH 7 and 30 degrees Celsius). Kcat is 177 sec(-1) for lyase activity (at pH 7.5 and 22 degrees Celsius). Kcat is 78 min(-1) for mutase activity (at pH 7 and 30 degrees Celsius). Kcat is 106 min(-1) for lyase activity (at pH 7 and 30 degrees Celsius).3 Publications

  1. KM=1.05 µM for isochorismate (at pH 7.5 and 30 degrees Celsius)1 Publication
  2. KM=4.3 µM for isochorismate (at pH 7.5 and 22 degrees Celsius)1 Publication
  3. KM=12.5 µM for isochorismate (at pH 7 and 30 degrees Celsius)1 Publication
  4. KM=120 µM for chorismate (at pH 7.5 and 22 degrees Celsius)1 Publication
  5. KM=150 µM for chorismate (at pH 7 and 30 degrees Celsius)1 Publication
  1. Vmax=0.049 µmol/min/mg enzyme for isochorismate pyruvate lyase activity (at pH 7 and 30 degrees Celsius)1 Publication
  2. Vmax=0.034 µmol/min/mg enzyme for chorismate mutase activity (at pH 7 and 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6.8.1 Publication

Pathwayi: salicylate biosynthesis

This protein is involved in the pathway salicylate biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway salicylate biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141Substrate2 Publications
Binding sitei31 – 311Substrate3 Publications
Binding sitei42 – 421Substrate2 Publications
Binding sitei90 – 901Substrate3 Publications

GO - Molecular functioni

  • carbon-oxygen lyase activity Source: UniProtKB
  • chorismate mutase activity Source: UniProtKB

GO - Biological processi

  • chorismate metabolic process Source: InterPro
  • pyochelin biosynthetic process Source: UniProtKB
  • salicylic acid biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15305.
BRENDAi4.2.99.21. 5087.
SABIO-RKQ51507.
UniPathwayiUPA00025.

Names & Taxonomyi

Protein namesi
Recommended name:
Isochorismate pyruvate lyase1 Publication (EC:4.2.99.214 Publications)
Short name:
IPL1 Publication
Alternative name(s):
Chorismate mutase1 Publication (EC:5.4.99.53 Publications)
Short name:
CM1 Publication
Salicylate biosynthesis protein1 Publication
Gene namesi
Name:pchB1 Publication
Ordered Locus Names:PA4230
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

PseudoCAPiPA4230.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371A → I: Increases the rate constant for the mutase activity by a factor of 1000, and also increases the lyase catalytic efficiency by a factor of 6. 1 Publication
Mutagenesisi42 – 421K → A: Active across the entire pH range from 4 to 9. 11-fold reduction of the affinity for isochorismate and 7-fold reduction of the catalytic efficiency for lyase activity. 6-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity. 2 Publications
Mutagenesisi42 – 421K → E: Loss of both lyase and mutase activity at any pH tested. 2 Publications
Mutagenesisi42 – 421K → H: At pH 5, 15-fold reduction of the affinity for isochorismate, but only a slight reduction of the catalytic efficiency for lyase activity. At pH 7.5, 13-fold reduction of the affinity for isochorismate and 4-fold reduction of the catalytic efficiency for lyase activity. At pH 5, strong reduction of the affinity for chorismate, but only a 2-fold reduction of the catalytic efficiency for mutase activity. At pH 7.5, strong reduction of the affinity for chorismate, but only a slight reduction of the catalytic efficiency for mutase activity. 2 Publications
Mutagenesisi42 – 421K → Q: Loss of mutase activity. 15-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity. 1 Publication
Mutagenesisi43 – 431A → P: Slight reduction of the affinity for isochorismate and of the catalytic efficiency for isochorismate-pyruvate lyase activity. Slight reduction of the affinity for chorismate and of the catalytic efficiency for mutase activity. 1 Publication
Mutagenesisi87 – 871I → T: 4-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity. 4-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Isochorismate pyruvate lyasePRO_0000119198Add
BLAST

Proteomic databases

PaxDbiQ51507.

Expressioni

Inductioni

Repressed by iron.1 Publication

Interactioni

Subunit structurei

Dimer of dimers.4 Publications

Protein-protein interaction databases

STRINGi208964.PA4230.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Helixi10 – 3829Combined sources
Helixi39 – 413Combined sources
Helixi45 – 473Combined sources
Helixi51 – 6717Combined sources
Helixi72 – 9625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H9CX-ray2.35A/B1-99[»]
2H9DX-ray1.95A/B/C/D1-101[»]
3HGWX-ray2.25A/B/C/D1-98[»]
3HGXX-ray2.50A/B1-99[»]
3REMX-ray1.95A/B1-101[»]
3RETX-ray1.79A/B1-101[»]
ProteinModelPortaliQ51507.
SMRiQ51507. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51507.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 9491Chorismate mutasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chorismate mutase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105VIA. Bacteria.
COG1605. LUCA.
HOGENOMiHOG000217291.
InParanoidiQ51507.
KOiK04782.
OMAiASRFKPD.
PhylomeDBiQ51507.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR008241. Isochorismate_pyruvate-lyase.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF029775. Isochor_pyr_lyas. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01803. CM-like. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q51507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPEDCTGL ADIREAIDRI DLDIVQALGR RMDYVKAASR FKASEAAIPA
60 70 80 90 100
PERVAAMLPE RARWAEENGL DAPFVEGLFA QIIHWYIAEQ IKYWRQTRGA

A
Length:101
Mass (Da):11,432
Last modified:December 8, 2000 - v2
Checksum:i97AE6DCE7A6ABD7D
GO

Sequence cautioni

The sequence CAA57968 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82644 Genomic DNA. Translation: CAA57968.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG07618.1.
PIRiA83117.
S60202. S58228.
RefSeqiNP_252920.1. NC_002516.2.
WP_003106950.1. NZ_ASJY01000704.1.

Genome annotation databases

EnsemblBacteriaiAAG07618; AAG07618; PA4230.
GeneIDi881846.
KEGGipae:PA4230.
PATRICi19843150. VBIPseAer58763_4431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82644 Genomic DNA. Translation: CAA57968.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG07618.1.
PIRiA83117.
S60202. S58228.
RefSeqiNP_252920.1. NC_002516.2.
WP_003106950.1. NZ_ASJY01000704.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H9CX-ray2.35A/B1-99[»]
2H9DX-ray1.95A/B/C/D1-101[»]
3HGWX-ray2.25A/B/C/D1-98[»]
3HGXX-ray2.50A/B1-99[»]
3REMX-ray1.95A/B1-101[»]
3RETX-ray1.79A/B1-101[»]
ProteinModelPortaliQ51507.
SMRiQ51507. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4230.

Proteomic databases

PaxDbiQ51507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07618; AAG07618; PA4230.
GeneIDi881846.
KEGGipae:PA4230.
PATRICi19843150. VBIPseAer58763_4431.

Organism-specific databases

PseudoCAPiPA4230.

Phylogenomic databases

eggNOGiENOG4105VIA. Bacteria.
COG1605. LUCA.
HOGENOMiHOG000217291.
InParanoidiQ51507.
KOiK04782.
OMAiASRFKPD.
PhylomeDBiQ51507.

Enzyme and pathway databases

UniPathwayiUPA00025.
BioCyciMetaCyc:MONOMER-15305.
BRENDAi4.2.99.21. 5087.
SABIO-RKQ51507.

Miscellaneous databases

EvolutionaryTraceiQ51507.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR008241. Isochorismate_pyruvate-lyase.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF029775. Isochor_pyr_lyas. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01803. CM-like. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCHB_PSEAE
AccessioniPrimary (citable) accession number: Q51507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: September 7, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.