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mpaA

Gene
mpaA
Protein
Polyprenyl transferase mapA
Organism
Penicillium brevicompactum
Length
315 amino acids
Function
Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world (PubMed:21398490, PubMed:22544261, PubMed:25630520). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the polyketide synthase mpaC (PubMed:21398490). 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by mpaDE (PubMed:22544261). MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB) (PubMed:22544261). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB is then converted to DHMP (PubMed:22544261). The next step is the prenylation of DHMP by the prenyltransferase mpaA to yield farnesyl-DHDMP (PubMed:25630520). Farnesyl-DHDMP might be a substrate of mpaH for transformation into demethylmycophenolic acid (DMMPA) (PubMed:25630520). Finally, the O-methyltransferase mpaG catalyzes the methylation DMMPA to form MPA (PubMed:25630520).
Similarity
Belongs to the UbiA prenyltransferase family.
Mass
35.969 kDa
Sequence
MTNAVEDSGPRDLLFLLISTSRFNRYMPYYTMMAAESLSIEFILYKAGLCFVHCLLLCGAGNTWNDLVDRDIDARVARTKMRPLASGKVTLTEALLWMTGQYFLSVKMLDLILDGRNIWSLMLPLTASIMLYPYLKRPIFSKVFVYPQYILGLAIGYPAITGWASITGSEEPLGDIIKHCIPICLLVFFWCVYFNTAYSHQDSVDDRKMNINSAYVIAGQRIRLFLAFLSVLPLLTIPYIISTINSPWLWVSWMATWTVSIIMQIAQFDSQKLESGGRIHWDNFLLGLWTIAACMVEVGLQKVEFWKNVEGYIKL

Gene
mpaA
Protein
Murein peptide amidase A
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
248 amino acids
Function
Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide.
Similarity
Belongs to the peptidase M14 family.
Mass
27.573 kDa
Sequence
MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL

Gene
mpaA
Protein
Murein peptide amidase A
Organism
Escherichia coli O157:H7
Length
242 amino acids
Function
Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap.
Similarity
Belongs to the peptidase M14 family.
Mass
26.558 kDa
Sequence
MTVTRPRAERGAFPPGTEHYGRSLLGAPLIWFPAPAASRESGLILAGTHGDENSSVVTLSCALRTLTPSLRRHHVVLCVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQALCQLIHRIQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAEFPPISSDEASEKYLFAMANLLRWHPKDAIRPS

Gene
mpaA
Protein
Murein peptide amidase A
Organism
Escherichia coli (strain K12)
Length
242 amino acids
Function
Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap (PubMed:12511517, PubMed:22970852). Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap (PubMed:22970852). Cannot hydrolyze murein tetrapeptide (PubMed:22970852).
Similarity
Belongs to the peptidase M14 family.
Mass
26.558 kDa
Sequence
MTVTRPRAERGAFPPGTEHYGRSLLGAPLIWFPAPAASRESGLILAGTHGDENSSVVTLSCALRTLTPSLRRHHVVLCVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQALCQLIHRIQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAEFPPISSDEASEKYLFAMANLLRWHPKDAIRPS