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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Bd4aq6b_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Cd4aq6c_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Dd4aq6d_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Ed4aq6e_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Gd4aq6g_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Hd4aq6h_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Id4aq6i_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Ld4aq6l_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Ad4aq6a_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Fd4aq6f_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Jd4aq6j_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Kd4aq6k_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
LSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
JSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
KSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BHgmA_2nde4aq6B3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
BHgmA_1ste4aq6B2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
CHgmA_2nde4aq6C3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
CHgmA_1ste4aq6C2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
DHgmA_2nde4aq6D3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
DHgmA_1ste4aq6D2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
EHgmA_2nde4aq6E3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
EHgmA_1ste4aq6E2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
GHgmA_2nde4aq6G3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
GHgmA_1ste4aq6G2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
HHgmA_2nde4aq6H3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
HHgmA_1ste4aq6H2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
IHgmA_2nde4aq6I3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
IHgmA_1ste4aq6I2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
LHgmA_2nde4aq6L3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
LHgmA_1ste4aq6L2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
AHgmA_2nde4aq6A3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
AHgmA_1ste4aq6A2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
FHgmA_2nde4aq6F3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
FHgmA_1ste4aq6F2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
JHgmA_2nde4aq6J3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
JHgmA_1ste4aq6J2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
KHgmA_2nde4aq6K3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
KHgmA_1ste4aq6K2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
C2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
D2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
E2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
G2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
H2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
I2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
L2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
A2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
F2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
J2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
K2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF04209Homogentisate 1,2-dioxygenase C-terminal (HgmA_C)Homogentisate 1,2-dioxygenase C-terminalHomogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangem ...Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers [1]. This entry represents the C-terminal active site domain.
Domain
A, B, C, D, E
PF20510Homogentisate 1,2-dioxygenase N-terminal (HgmA_N)Homogentisate 1,2-dioxygenase N-terminalHomogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangem ...Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers [1]. This entry represents the N-terminal domain which forms a jelly roll of beta-strands [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
HOMOGENTISATE 1,2-DIOXYGENASE

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D, E
IPR022950Homogentisate 1,2-dioxygenase, bacterialFamily
A, B, C, D, E
IPR014710RmlC-like jelly roll foldHomologous Superfamily
A, B, C, D, E
IPR046452Homogentisate 1,2-dioxygenase, N-terminal domainDomain
A, B, C, D, E
IPR011051RmlC-like cupin domain superfamilyHomologous Superfamily
A, B, C, D, E
IPR046451Homogentisate 1,2-dioxygenase, C-terminal domainDomain
A, B, C, D, E
IPR005708Homogentisate 1,2-dioxygenaseFamily