Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins
Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.
Feature 1:heme binding site [chemical binding site]
Evidence:
Structure:1CQX: the globin domain of Alcaligenes eutrophus FHP binds heme; contacts at 4A
Comment:a phospholipid-binding site is located adjacent to the heme molecule; the heme interacts with the phospholipid and residues of the globin domain
Comment:also based on the binding of heme to other flavohemoglobins with structure
Jiyao W et al.(2023). "The conserved domain database in 2023.",