Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry Q88H25 for Pseudomonas putida KT2440 mvaB
Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
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Structures of two bacterial HMG-CoA lyases identify a conserved divalent-cation site in the catalytic center.
"the catalytic center contains a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel"
The Pseudomonas aeruginosa liuE gene encodes the 3-hydroxy-3-methylglutaryl coenzyme A lyase, involved in leucine and acyclic terpene catabolism.
Identification of genes and proteins necessary for catabolism of acyclic terpenes and leucine/isovalerate in Pseudomonas aeruginosa.
OpenScientist gene research for PSEPK mvaB
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The report supports MvaB as the principal HMG-CoA lyase candidate while retaining uncertainty about the PP_3394 paralog and direct KT2440 biochemistry.
"No direct biochemistry on PP_3540 itself."
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The provider reports high sequence identity between MvaB and characterized P. aeruginosa LiuE.
"| mvaB (PP_3540) vs. *P. aeruginosa* LiuE/PA2011 (characterized HMG-CoA lyase) | **78.6%** |"
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The provider reports that mvaB is genomically separated from the clustered upstream leucine-catabolism genes.
"By contrast, **mvaB/PP_3540 is located ~500 genes away** from this cluster"