pyridoxal 5'-phosphate synthase catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
57-261
2.12e-108
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
:
Pssm-ID: 273138 Cd Length: 190 Bit Score: 310.97 E-value: 2.12e-108
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
57-261
2.12e-108
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 310.97 E-value: 2.12e-108
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
33-261
2.26e-106
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 306.73 E-value: 2.26e-106
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
77-153
2.36e-25
Pyridoxamine 5'-phosphate oxidase; 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 pfam01243 and pfam10590. 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.
Pssm-ID: 426149 [Multi-domain] Cd Length: 88 Bit Score: 95.78 E-value: 2.36e-25
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
57-261
2.12e-108
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 310.97 E-value: 2.12e-108
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
33-261
2.26e-106
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 306.73 E-value: 2.26e-106
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
77-153
2.36e-25
Pyridoxamine 5'-phosphate oxidase; 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 pfam01243 and pfam10590. 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.
Pssm-ID: 426149 [Multi-domain] Cd Length: 88 Bit Score: 95.78 E-value: 2.36e-25
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
206-261
2.49e-17
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of the two dimerization regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In Swiss:P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule.To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity.
Pssm-ID: 463161 Cd Length: 42 Bit Score: 73.31 E-value: 2.49e-17
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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