Pyridoxine/pyridoxamine 5'-phosphate oxidase (P0AFI7)

Identification
Name:Pyridoxine/pyridoxamine 5'-phosphate oxidase
Synonyms:
  • PNP/PMP oxidase
  • PNPOx
  • Pyridoxal 5'-phosphate synthase
Gene Name:pdxH
Enzyme Class:
Biological Properties
General Function:Coenzyme transport and metabolism
Specific Function:Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Oxygen + 1.0Pyridoxine 5'-phosphate → 1.0Hydrogen peroxide + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Pyridoxamine 5'-phosphate + 1.0Water + 1.0Oxygen ↔ 1.0Pyridoxal 5'-phosphate + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Pyridoxine 5'-phosphate + 1.0Oxygen ↔ 1.0Hydrogen peroxide + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Pyridoxamine + 1.0Water + 1.0Oxygen ↔ 1.0Pyridoxal + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Pyridoxine + 1.0Oxygen ↔ 1.0Pyridoxal + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Pyridoxamine 5'-phosphate + 1.0Water + 1.0Oxygen + 1.0Pyridoxine 5'-phosphate ↔ 1.0Pyridoxal 5'-phosphate + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Oxygen + 1.0Pyridoxine 5'-phosphate → 1.0Hydrogen peroxide + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Pyridoxamine 5'-phosphate + 1.0Water + 1.0Oxygen ↔ 1.0Pyridoxal 5'-phosphate + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxygen + 1.0Pyridoxamine 5'-phosphate → 1.0Hydrogen peroxide + 1.0Ammonium + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Pyridoxamine 5'-phosphate + 1.0Water + 1.0Oxygen → 1.0Pyridoxal 5'-phosphate + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB01545PyridoxalMetaboCard
ECMDB01491Pyridoxal 5'-phosphateMetaboCard
ECMDB01431PyridoxamineMetaboCard
ECMDB01555Pyridoxamine 5'-phosphateMetaboCard
ECMDB00239PyridoxineMetaboCard
ECMDB01319Pyridoxine 5'-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
FMN binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH2 group of donors
oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
pyridoxamine-phosphate oxidase activity
Process
metabolic process
oxidation reduction
pyridoxine biosynthetic process
pyridoxine metabolic process
small molecule metabolic process
vitamin B6 metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b1638
Gene OrientationCounterclockwise
Centisome Percentage:36.97
Left Sequence End1715375
Right Sequence End1716031
Gene Sequence:
>657 bp
GTGCAACGAGCGCGTTGTTATCTGATAGGTGAAACGGCGGTAGTGCTGGAACTGGAACCG
CCGGTGACGCTGGCTAGCCAGAAACGGATCTGGCGACTGGCGCAGCGTCTGGTGGATATG
CCGAATGTGGTTGAAGCCATTCCCGGCATGAACAATATCACGGTGATTTTGCGTAATCCT
GAGTCGCTGGCGCTGGATGCCATAGAGCGTTTGCAACGCTGGTGGGAGGAGAGCGAGGCG
CTGGAGCCGGAGTCTCGCTTTATTGAAATTCCGGTGGTTTACGGTGGTGCAGGCGGACCG
GATTTGGCGGTGGTCGCGGCGCATTGCGGGTTGAGCGAAAAACAGGTTGTTGAATTGCAC
TCCTCCGTGGAATACGTGGTCTGGTTTTTAGGTTTTCAACCGGGCTTCCCGTATCTCGGG
AGTTTGCCGGAACAACTACACACGCCACGGCGCGCTGAACCGCGCTTACTCGTTCCGGCA
GGTTCTGTCGGGATCGGCGGGCCGCAGACTGGTGTTTATCCGCTGGCAACGCCGGGTGGC
TGGCAGTTGATTGGTCATACCTCACTCAGCCTGTTTGATCCGGCGCGTGACGAACCCATC
TTATTACGTCCGGGAGACAGCGTGCGCTTTGTACCGCAGAAGGAGGGAGTATGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:218
Protein Molecular Weight:25545
Protein Theoretical pI:10
PDB File:1WV4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyridoxine/pyridoxamine 5'-phosphate oxidase
MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDE
HGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAER
LSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGG
FRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP
References
External Links:
ResourceLink
Uniprot ID:P0AFI7
Uniprot Name:PDXH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062307
PDB ID:1WV4
Ecogene ID:EG11487
Ecocyc:EG11487
ColiBase:b1638
Kegg Gene:b1638
EchoBASE ID:EB1450
CCDB:PDXH_ECOLI
BacMap:16129596
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • di Salvo, M. L., Ko, T. P., Musayev, F. N., Raboni, S., Schirch, V., Safo, M. K. (2002). "Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase." J Mol Biol 315:385-397. Pubmed: 11786019
  • Di Salvo, M., Yang, E., Zhao, G., Winkler, M. E., Schirch, V. (1998). "Expression, purification, and characterization of recombinant Escherichia coli pyridoxine 5'-phosphate oxidase." Protein Expr Purif 13:349-356. Pubmed: 9693059
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Lam, H. M., Winkler, M. E. (1992). "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations." J Bacteriol 174:6033-6045. Pubmed: 1356963
  • Safo, M. K., Mathews, I., Musayev, F. N., di Salvo, M. L., Thiel, D. J., Abraham, D. J., Schirch, V. (2000). "X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution." Structure 8:751-762. Pubmed: 10903950
  • Safo, M. K., Musayev, F. N., di Salvo, M. L., Schirch, V. (2001). "X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution." J Mol Biol 310:817-826. Pubmed: 11453690
  • Safo, M. K., Musayev, F. N., Schirch, V. (2005). "Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme." Acta Crystallogr D Biol Crystallogr 61:599-604. Pubmed: 15858270
  • Zhao, G., Winkler, M. E. (1995). "Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12." J Bacteriol 177:883-891. Pubmed: 7860596