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UniProt functional annotation for Q51507 | ||
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| UniProt code: Q51507. |
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| Organism: | |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. |
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| Function: | |
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. {ECO:0000269|PubMed:11937513, ECO:0000269|PubMed:16248620, ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784, ECO:0000269|PubMed:7500944}. |
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| Catalytic activity: | |
Reaction=isochorismate = pyruvate + salicylate; Xref=Rhea:RHEA:27874, ChEBI:CHEBI:15361, ChEBI:CHEBI:29780, ChEBI:CHEBI:30762; EC=4.2.99.21; Evidence={ECO:0000269|PubMed:11937513, ECO:0000269|PubMed:16248620, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784}; |
| Catalytic activity: | |
Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:11937513, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784}; |
| Activity regulation: | |
Inhibited by endo-oxabicyclic diacid resembling to the conformation of the transition state. {ECO:0000269|PubMed:11937513}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=1.05 uM for isochorismate (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16248620}; KM=4.3 uM for isochorismate (at pH 7.5 and 22 degrees Celsius) {ECO:0000269|PubMed:19432488}; KM=12.5 uM for isochorismate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:11937513}; KM=120 uM for chorismate (at pH 7.5 and 22 degrees Celsius) {ECO:0000269|PubMed:19432488}; KM=150 uM for chorismate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:11937513}; Vmax=0.049 umol/min/mg enzyme for isochorismate pyruvate lyase activity (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:11937513}; Vmax=0.034 umol/min/mg enzyme for chorismate mutase activity (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:11937513}; Note=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). {ECO:0000269|PubMed:11937513, ECO:0000269|PubMed:16248620, ECO:0000269|PubMed:19432488}; pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:11937513}; |
| Pathway: | |
Siderophore biosynthesis; salicylate biosynthesis. {ECO:0000269|PubMed:7500944}. |
| Subunit: | |
Dimer of dimers. {ECO:0000269|PubMed:11937513, ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784}. |
| Induction: | |
Repressed by iron. {ECO:0000305|PubMed:7500944}. |
| Sequence caution: | |
Sequence=CAA57968.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.