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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad3zdsa_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Bd3zdsb_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Cd3zdsc_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Ed3zdse_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Fd3zdsf_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Gd3zdsg_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Hd3zdsh_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Id3zdsi_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Jd3zdsj_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Kd3zdsk_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Ld3zdsl_ All beta proteins Double-stranded beta-helix RmlC-like cupins automated matches automated matches (Pseudomonas putida KT2440 ) [TaxId: 160488 ], SCOPe (2.08)
Dd3zdsd_ 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)
ASCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
BSCOP2 FamilyHomogentisate dioxygenase 8088132 4002879 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2 (2022-06-29)
CSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
FSCOP2B 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)
JSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
KSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
LSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyRmlC-like cupins 8088133 3001825 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AHgmA_2nde3zdsA3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
AHgmA_1ste3zdsA2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
BHgmA_2nde3zdsB3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
BHgmA_1ste3zdsB2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
CHgmA_2nde3zdsC3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
CHgmA_1ste3zdsC2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
EHgmA_2nde3zdsE3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
EHgmA_1ste3zdsE2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
FHgmA_2nde3zdsF3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
FHgmA_1ste3zdsF2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
GHgmA_2nde3zdsG3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
GHgmA_1ste3zdsG2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
HHgmA_2nde3zdsH3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
HHgmA_1ste3zdsH2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
IHgmA_2nde3zdsI3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
IHgmA_1ste3zdsI2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
JHgmA_2nde3zdsJ3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
JHgmA_1ste3zdsJ2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
KHgmA_2nde3zdsK3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
KHgmA_1ste3zdsK2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
LHgmA_2nde3zdsL3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
LHgmA_1ste3zdsL2 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_1stECOD (1.6)
DHgmA_2nde3zdsD3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: HgmA_2ndECOD (1.6)
DHgmA_1ste3zdsD2 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)
A2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
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)
E2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
F2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
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)
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)
L2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)
D2.60.120.10 Mainly Beta Sandwich Jelly Rolls Jelly RollsCATH (4.3.0)

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