Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Bd2ohjb2 Alpha and beta proteins (a/b) Flavodoxin-like Flavoproteins automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
Bd2ohjb1 Alpha and beta proteins (a+b) Metallo-hydrolase/oxidoreductase Metallo-hydrolase/oxidoreductase automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
C [auth D]d2ohjd2 Alpha and beta proteins (a/b) Flavodoxin-like Flavoproteins automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
C [auth D]d2ohjd1 Alpha and beta proteins (a+b) Metallo-hydrolase/oxidoreductase Metallo-hydrolase/oxidoreductase automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
Ad2ohja2 Alpha and beta proteins (a/b) Flavodoxin-like Flavoproteins automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
Ad2ohja1 Alpha and beta proteins (a+b) Metallo-hydrolase/oxidoreductase Metallo-hydrolase/oxidoreductase automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
D [auth E]d2ohje2 Alpha and beta proteins (a/b) Flavodoxin-like Flavoproteins automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)
D [auth E]d2ohje1 Alpha and beta proteins (a+b) Metallo-hydrolase/oxidoreductase Metallo-hydrolase/oxidoreductase automated matches automated matches (Methanothermobacter thermautotrophicus ) [TaxId: 145262 ], SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BLactamase_B_1e2ohjB1 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: Lactamase_B_1ECOD (1.6)
BFlavodoxin_1e2ohjB2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: Flavodoxin_1ECOD (1.6)
C [auth D]Lactamase_B_1e2ohjD1 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: Lactamase_B_1ECOD (1.6)
C [auth D]Flavodoxin_1e2ohjD2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: Flavodoxin_1ECOD (1.6)
ALactamase_B_1e2ohjA1 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: Lactamase_B_1ECOD (1.6)
AFlavodoxin_1e2ohjA2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: Flavodoxin_1ECOD (1.6)
D [auth E]Lactamase_B_1e2ohjE1 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: Lactamase_B_1ECOD (1.6)
D [auth E]Flavodoxin_1e2ohjE2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: Flavodoxin_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A,
B,
C [auth D],
D [auth E]
PF19583ODP family beta lactamase (ODP)ODP family beta lactamaseThe ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ...The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.
Domain
A,
B,
C [auth D],
D [auth E]
PF00258Flavodoxin (Flavodoxin_1)Flavodoxin- Domain