Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AHPPD_N_likee2r5vA7 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: HPPD_N_likeECOD (1.6)
AGlyoxalase_10e2r5vA5 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_10ECOD (1.6)
AGlyoxalase_4_2e2r5vA1 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_4_2ECOD (1.6)
AGlyoxalase_5_Ce2r5vA6 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_5_CECOD (1.6)
BHPPD_N_likee2r5vB10 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: HPPD_N_likeECOD (1.6)
BGlyoxalase_10e2r5vB8 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_10ECOD (1.6)
BGlyoxalase_4_2e2r5vB1 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_4_2ECOD (1.6)
BGlyoxalase_5_Ce2r5vB9 A: a+b two layersX: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenaseF: Glyoxalase_5_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.10.180.10 Alpha Beta Roll 2,3-Dihydroxybiphenyl 1,2-Dioxygenase domain 1CATH (4.3.0)
B3.10.180.10 Alpha Beta Roll 2,3-Dihydroxybiphenyl 1,2-Dioxygenase domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00903Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily- Domain
A, B
PF14696Hydroxyphenylpyruvate dioxygenase, HPPD, N-terminal (Glyoxalase_5)Hydroxyphenylpyruvate dioxygenase, HPPD, N-terminalThis domain is one of two barrel-shaped regions that together form the active enzyme, 4-hydroxyphenylpyruvic acid dioxygenase, EC:1.13.11.27. As can be deduced from the disposition of the various Glyoxalase families, _2, _3 and _4 in Pfam, Pfam:PF009 ...This domain is one of two barrel-shaped regions that together form the active enzyme, 4-hydroxyphenylpyruvic acid dioxygenase, EC:1.13.11.27. As can be deduced from the disposition of the various Glyoxalase families, _2, _3 and _4 in Pfam, Pfam:PF00903, Pfam:PF12681, Pfam:PF13468, Pfam:PF13669, these two regions are similar to be indicative of a gene-duplication event. At the individual sequence level slight differences in conformation have given rise to slightly different functions. In the case of UniProt:P80064, 4-hydroxyphenylpyruvic acid dioxygenase catalyses the formation of homogentisate from 4-hydroxyphenylpyruvate, and the pyruvate part of the HPPD substrate (4-hydroxyphenylpyruvate), derived from L-tyrosine, and the O2 molecule occupy the three free coordination sites of the catalytic iron atom in the C-terminal domain. In plants and photosynthetic bacteria, the tyrosine degradation pathway is crucial because homogentisate, a tyrosine degradation product, is a precursor for the biosynthesis of photosynthetic pigments, such as quinones or tocopherols [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
PCZA361.1 -