7OUC

Crystal structure of the flavoprotein monooxygenase GrhO5 from griseorhodin A biosynthesis


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth AAA]PRK06126_2nde7oucAAA2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PRK06126_2ndECOD (1.6)
A [auth AAA]FAD_binding_3_1ste7oucAAA1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: FAD_binding_3_1stECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth AAA]PF21274Aromatic-ring hydroxylase, C-terminal (Rng_hyd_C)Aromatic-ring hydroxylase, C-terminalThis is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved ...This is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved in folding and stability [6] as it lacks the catalytic cysteine residues of thioredoxin, therefore, is not likely to have a redox function [1].
Domain
A [auth AAA]PF01494FAD binding domain (FAD_binding_3)FAD binding domain- Family