GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000108

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:22272184

Substrate specificity within a family of outer membrane carboxylate channels

The OprD family is redefined as Occ (outer membrane carboxylate) channels; OccD1 (historically OprD) is the family archetype associated with transport of basic amino acids, with selectivity shaped by a constriction formed by extracellular loops and conserved charged residues.

PMID:28981745

Structure, function and regulation of Pseudomonas aeruginosa porins

Authoritative review of Pseudomonas porins describing the OprD/Occ family split into OccD (basic amino acid uptake) and OccK (carboxylate/cyclic molecule uptake) subfamilies, and emphasizing the low intrinsic permeability of the Pseudomonas outer membrane.

PMID:16352820

Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa

OprD-subfamily porins mediate uptake of amino acids and related molecules (e.g., dipeptides) in Pseudomonas, with substrate-inducible expression.

PMID:30557364

The CbrB regulon - promoter dissection reveals novel insights into the cbrAB expression network in Pseudomonas putida

In P. putida, the carbon-status response regulator CbrB binds the oprD (PP1206) promoter directly (EMSA), and PP1206 is part of the CbrB regulon, linking oprD expression to carbon/nitrogen status signaling.

PMID:22433058

The metabolic response of P. putida KT2442 producing high levels of polyhydroxyalkanoate under single- and multiple-nutrient-limited growth: highlights from a multi-level omics approach.

In P. putida KT2442 chemostats, the specific porin OprD (PP_1206) was induced under dual carbon-plus-nitrogen limitation; the authors note OprD is implicated in uptake of basic amino acids across the membrane.