_EC 1.4.3.5 Pyridoxal 5'-phosphate synthase. 17 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,574 PDB entries]
EC 1.4.-.- Acting on the CH-NH(2) group of donors. [356 PDB entries]
EC 1.4.3.- With oxygen as acceptor. [216 PDB entries]
EC 1.4.3.5 Pyridoxal 5'-phosphate synthase. [17 PDB entries]    
1ci0

Reaction: (1) Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). (2) Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2).
 


Pyridoxamine 5'-phosphate
+ H(2)O
+
O(2)
=
pyridoxal 5'-phosphate
+ NH(3)
+
H(2)O(2)

Pyridoxine 5'-phosphate
+
O(2)
=
pyridoxal 5'-phosphate
+
H(2)O(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Pmp oxidase. Pyridoxamine 5'-phosphate oxidase. Pyridoxamine phosphate oxidase. Pyridoxamine-phosphate oxidase. Pyridoxine (pyridoxamine) 5'-phosphate oxidase. Pyridoxine (pyridoxamine)phosphate oxidase.
Cofactor(s): Fmn.
 

FMN
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves Ec 1.2.1.72, Ec 1.1.1.290, Ec 2.6.1.52, Ec 1.1.1.262, Ec 2.6.99.2 and Ec 1.4.3.5.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 17 PDB entries in enzyme class E.C.1.4.3.5

  PDB code Protein
1ci0
Pnp oxidase from saccharomyces cerevisiae
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (205 residues) CATH domain: 2.30.110.10
Bound ligand:   Het Group FMN corresponds to enzyme cofactor FMN
1dnl
X-ray structure of escherichia coli pyridoxine 5'-phosphate complexed with fmn at 1.8 angstrom resolution
Source: Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (199 residues) CATH domain: 2.30.110.10
Bound ligand:   Het Group FMN corresponds to enzyme cofactor FMN
1g76
X-ray structure of escherichia coli pyridoxine 5'-phosphate complexed with pyridoxal 5'-phosphate at 2.0 a resolution
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (199 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1g77
X-ray structure of escherichia coli pyridoxine 5`-phosphate complexed with pyridoxal 5'-phosphate at 2.0 a resolution
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (199 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1g78
X-ray structure of escherichia coli pyridoxine 5'-phosphate complexed with pyridoxal 5'-phosphate at 2.0 a resolution
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (199 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1g79
X-ray structure of escherichia coli pyridoxine 5'-phosphate complexed with pyridoxal 5'-phosphate at 2.0 a resolution
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (199 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1jnw
Active site structure of e. Coli pyridoxine 5'-phosphate oxi
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (214 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1nrg
Structure and properties of recombinant human pyridoxine-5'- oxidase
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: human. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
1w9a
Crystal structure of rv1155 from mycobacterium tuberculosis
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
Chains: A, B (142 residues) CATH domain: 2.30.110.10
1wv4
X-ray structure of escherichia coli pyridoxine 5'-phosphate oxidase in tetragonal crystal form
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (162 residues) CATH domain: 2.30.110.10
Bound ligand:   Het Group FMN corresponds to enzyme cofactor FMN
1xxo
X-ray crystal structure of mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase at 1.8 a resolution
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: rv1155. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (143 residues) CATH domain: 2.30.110.10
1y30
X-ray crystal structure of mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase complexed with flavin mononucleotide at 2.2 a resolution
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: rv1155. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (143 residues) CATH domain: 2.30.110.10
2a2j
Crystal structure of a putative pyridoxine 5'-phosphate oxid (rv2607) from mycobacterium tuberculosis
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (203 residues) CATH domain: 2.30.110.10
2aq6
X-ray crystal structure of mycobacterium tuberculosis pyrido phosphate oxidase complexed with pyridoxal 5'-phosphate at resolution
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: rv1155. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (143 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
3hy8
Crystal structure of human pyridoxine 5'-phosphate oxidase r mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pnpo. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (211 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group PLP corresponds to enzyme product pyridoxal
  Het Group PLP corresponds to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN
4hmw
Crystal structure of phzg from burkholderia lata 383
Source: Burkholderia. Burkholderia cepacia. Organism_taxid: 269483. Strain: 383. Gene: bcep18194_b1572. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (202 residues) CATH domain: 2.30.110.10
Bound ligand:   Het Group FMN corresponds to enzyme cofactor FMN
4hmx
Crystal structure of phzg from burkholderia lata 383 in comp tetrahydrophenazine-1-carboxylic acid
Source: Burkholderia. Organism_taxid: 269483. Strain: 383. Gene: bcep18194_b1572. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (202 residues) CATH domain: 2.30.110.10
Bound ligands:   Het Group WUB is 43.48% similar to enzyme reactant Pyridoxamine
  Het Group WUB is 43.48% similar to enzyme reactant Pyridoxine
  Het Group FMN corresponds to enzyme cofactor FMN