GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:PSEPK/pqqD2/pqqD2-uniprot.txt

UniProtKB entry for pqqD2 (PqqA binding protein 2)

"RecName: Full=PqqA binding protein 2"
"FUNCTION: Functions as a PqqA binding protein and presents PqqA to"
"PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis."
"SUBUNIT: Monomer. Interacts with PqqE."
"DR GO; GO:0048038; F:quinone binding; IEA:InterPro."

file:PSEPK/pqqD2/pqqD2-goa.tsv

QuickGO GOA annotations for pqqD2

"GO:0018189 pyrroloquinoline quinone biosynthetic process"
"GO:0048038 quinone binding"

file:PSEPK/pqqD2/pqqD2-deep-research-asta.md

Asta retrieval report for pqqD2 (Q88JG8 / PP_2681), Pseudomonas putida KT2440

"Protein Description:** RecName: Full=PqqA binding protein 2"
"Gene Information:** Name=pqqD2; OrderedLocusNames=PP_2681;"
"Key Domains:** PQQD. (IPR008792); PqqD_bac. (IPR022479); PqqD_sf. (IPR041881); PqqD (PF05402)"

file:PSEPK/pqqD2/pqqD2-deep-research-openscientist.md

OpenScientist research report for pqqD2 (Q88JG8, P. putida KT2440)

PMID:26961875

Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD.

"These results indicate that PqqE, in conjunction with PqqD, carries out the first step in PQQ biosynthesis"
"PqqD was shown to bind tightly to PqqA and to enter into a ternary complex with PqqE"