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UniProt functional annotation for Q8F3Q1 | ||
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| UniProt code: Q8F3Q1. |
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| Organism: | |
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601). |
| Taxonomy: | |
Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. |
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| Function: | |
Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate (PubMed:15292141, PubMed:18498255, PubMed:19351325). Shows strict substrate specificity for pyruvate. Cannot use alpha-ketoisovalerate, alpha-ketobutyrate, alpha- ketoisocaproate, alpha-ketoglutarate or glyoxylate (PubMed:15292141, PubMed:18498255). {ECO:0000269|PubMed:15292141, ECO:0000269|PubMed:18498255, ECO:0000269|PubMed:19351325}. |
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| Catalytic activity: | |
Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+); Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.182; Evidence={ECO:0000269|PubMed:15292141, ECO:0000269|PubMed:18498255, ECO:0000269|PubMed:19351325}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19046; Evidence={ECO:0000269|PubMed:15292141, ECO:0000269|PubMed:18498255, ECO:0000269|PubMed:19351325}; |
| Cofactor: | |
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18498255}; Note=Mn(2+) is the most effective activator, followed by Co(2+), Ca(2+), Mg(2+) and Ni(2+). {ECO:0000269|PubMed:18498255}; |
| Activity regulation: | |
Regulated by the end-product isoleucine via a feedback inhibition. The binding of isoleucine has inhibitory effects on the binding of both pyruvate and acetyl-CoA. May act via conformational change of the dimer interface of the regulatory domain, leading to inhibition of the catalytic reaction. {ECO:0000269|PubMed:19351325}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=43 uM for pyruvate {ECO:0000269|PubMed:15292141}; KM=60 uM for pyruvate {ECO:0000269|PubMed:18498255}; KM=1118 uM for acetyl-CoA {ECO:0000269|PubMed:18498255}; Note=kcat is 2.41 sec(-1) (PubMed:15292141). kcat is 10.3 sec(-1) with acetyl-CoA as substrate (PubMed:18498255). kcat is 9.13 sec(-1) with pyruvate as substrate (PubMed:18498255). {ECO:0000269|PubMed:15292141, ECO:0000269|PubMed:18498255}; Temperature dependence: Optimum temperature is 35-40 degrees Celsius. {ECO:0000269|PubMed:15292141}; |
| Pathway: | |
Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- oxobutanoate from pyruvate: step 1/3. {ECO:0000269|PubMed:15292141}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:18498255, ECO:0000269|PubMed:19351325}. |
| Induction: | |
Expression is repressed by isoleucine but not by leucine. {ECO:0000269|PubMed:15292141}. |
| Domain: | |
Contains a catalytic N-terminal domain and a C-terminal regulatory domain, linked together by a flexible region (PubMed:18498255, PubMed:19351325). The catalytic domain consists of a TIM barrel flanked by an extended C-terminal region. The active site is located at the center of the TIM barrel near the C-terminal ends of the beta-strands and is composed of conserved residues of the beta-strands of one subunit and the C-terminal region of the other (PubMed:18498255). {ECO:0000269|PubMed:18498255, ECO:0000269|PubMed:19351325}. |
| Similarity: | |
Belongs to the alpha-IPM synthase/homocitrate synthase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.