Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BPyr_redox_2_2e3h8iB2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2_2ECOD (1.6)
BPyr_redox_2e3h8iB5 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2ECOD (1.6)
APyr_redox_2_2e3h8iA2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2_2ECOD (1.6)
APyr_redox_2e3h8iA5 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.50.50.60 Alpha Beta 3-Layer(bba) Sandwich FAD/NAD(P)-binding domain FAD/NAD(P)-binding domainCATH (4.3.0)
A3.50.50.60 Alpha Beta 3-Layer(bba) Sandwich FAD/NAD(P)-binding domain FAD/NAD(P)-binding domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF07992Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2)Pyridine nucleotide-disulphide oxidoreductaseThis family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.Domain

InterPro: Protein Family Classification InterPro Database Homepage

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
sulfide:quinone oxidoreductase  M-CSA #320

Catalyses the oxidation of sulfides, such as hydrogen sulfide, with the help of a quinone to form sulfur globules. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur. This is an important step in anoxygenic bacterial photosynthesis.

Defined by 6 residues: CYS:A-129CYS:A-178ASP:A-215CYS:A-350ASP:A-353LYS:A-386
Some residues are not modelled and lack atomic coordinates. Visualization is not available.
Some residues are not modelled and lack atomic coordinates. Structure Motif searching is not available.
EC: 1.6.99.3 (PDB Primary Data)
EC: 1.8.5.4 (UniProt)