Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAsp_Arg_Hydroxe6rk9A1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: Asp_Arg_HydroxECOD (1.6)
ATPR_11_6e6rk9A2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_6ECOD (1.6)
BAsp_Arg_Hydroxe6rk9B1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: Asp_Arg_HydroxECOD (1.6)
BTPR_11_6e6rk9B2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_6ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.60.120.330 Mainly Beta Sandwich Jelly Rolls B-lactam Antibiotic, Isopenicillin N SynthaseCATH (utative)
B2.60.120.330 Mainly Beta Sandwich Jelly Rolls B-lactam Antibiotic, Isopenicillin N SynthaseCATH (utative)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF13432Tetratricopeptide repeat (TPR_16)Tetratricopeptide repeat- Repeat
A, B
PF05118Aspartyl/Asparaginyl beta-hydroxylase (Asp_Arg_Hydrox)Aspartyl/Asparaginyl beta-hydroxylaseIron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino a ...Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Aspartyl/asparaginyl beta-hydroxylase
ACA-LYS-ASP-GLY-LEU-GLY-GLU-TYR-THR-CYS-THR-SER-LEU-GLU-GLY-PHE-GLU---

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
DAL RESIDAA0111 , AA0191

PSI-MOD :  meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862