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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPNP-oxidase like8024935 4002129 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFMN-binding split barrel8037314 3000856 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyFMN-binding split barrel8037314 3000856 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APyrid_oxidase_2e2arzA2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrelF: Pyrid_oxidase_2ECOD (1.6)
ADUF2470e2arzA3 A: a+b two layersX: a+b domain in heme oxygenase (From Topology)H: a+b domain in heme oxygenase (From Topology)T: a+b domain in heme oxygenaseF: DUF2470ECOD (1.6)
BPyrid_oxidase_2e2arzB2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrelF: Pyrid_oxidase_2ECOD (1.6)
BDUF2470e2arzB3 A: a+b two layersX: a+b domain in heme oxygenase (From Topology)H: a+b domain in heme oxygenase (From Topology)T: a+b domain in heme oxygenaseF: DUF2470ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.30.110.10 Mainly Beta Roll Pnp Oxidase Chain ACATH (4.3.0)
A3.20.180.10 Alpha Beta Alpha-Beta Barrel Split barrel-like PNP-oxidase-likeCATH (4.3.0)
B2.30.110.10 Mainly Beta Roll Pnp Oxidase Chain ACATH (4.3.0)
B3.20.180.10 Alpha Beta Alpha-Beta Barrel Split barrel-like PNP-oxidase-likeCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF01243Pyridoxamine 5'-phosphate oxidase (Putative_PNPOx)Pyridoxamine 5'-phosphate oxidaseFamily of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, ...Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both Pfam:PF01243 and Pfam:PF10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown [1].
Domain
A, B
PF10615Domain of unknown function (DUF2470) (DUF2470)Domain of unknown function (DUF2470)This domain is found in a group of putative heme-iron utilisation proteins, such as HugZ. It can also be found in C-terminal of the glutamyl-tRNA reductase-binding (GluTRBP) protein from Arabidopsis [1]. GluTRBP is involved in the regulation of gluta ...This domain is found in a group of putative heme-iron utilisation proteins, such as HugZ. It can also be found in C-terminal of the glutamyl-tRNA reductase-binding (GluTRBP) protein from Arabidopsis [1]. GluTRBP is involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis [2]. GluTRBP is necessary for efficient photosynthetic electron transport in chloroplasts [3].
Domain

InterPro: Protein Family Classification InterPro Database Homepage