Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry C5CPT7 (PQQA_VARPS): Coenzyme PQQ synthesis protein A
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C5CPT7 (Vapar_3057) is a reviewed 24-residue PqqA precursor peptide in Variovorax paradoxus S110 containing the conserved Glu16-Tyr20 cross-linking site (FT CROSSLNK 16..20) required for pyrroloquinoline quinone biosynthesis.
"CC -!- FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ)
CC biosynthesis. PQQ is probably formed by cross-linking a specific
CC glutamate to a specific tyrosine residue and excising these residues
CC from the peptide. {ECO:0000255|HAMAP-Rule:MF_00656}."
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Residues 16 to 20 of Vapar_3057 (Glu16 and Tyr20 in MKWETPTATDLRFGFEITMYVSAR) form the pyrroloquinoline quinone (Glu-Tyr) cross-link site.
"FT CROSSLNK 16..20
FT /note="Pyrroloquinoline quinone (Glu-Tyr)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00656""
Complete genome sequence of the metabolically versatile plant growth-promoting endophyte Variovorax paradoxus S110.
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Reports the complete genome sequence of Variovorax paradoxus S110 encoding Vapar_3057 (pqqA).
"The complete genome sequence of V. paradoxus S110 is composed of 6,754,997 bp with 6,279 predicted protein-coding sequences within two circular chromosomes."
PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway.
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Demonstrates that PqqA is the conserved peptide substrate of the pqqA-E RiPP pathway whose glutamate and tyrosine side chains are cross-linked by PqqE after nanomolar binding of PqqA to the peptide chaperone PqqD in a ternary PqqA-PqqD-PqqE complex.
"Pyrroloquinoline quinone (PQQ) is a product of a ribosomally synthesized and post-translationally modified pathway consisting of five conserved genes, pqqA-E. PqqE is a radical S-adenosylmethionine (RS) protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA."
Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone.
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Reviews the complete PQQ biosynthetic pathway from the ribosomally synthesized precursor peptide PqqA, whose conserved glutamate and tyrosine residues supply the carbon-nitrogen skeleton of PQQ.
"The pqqA is translated into a short peptide that contains the fully conserved residues, glutamate and tyrosine; site-direct mutagenesis identified these two residues on PqqA as the best candidate for the precursor to PQQ (Figure 2A).[31]"