Q3KGY4 (PDXH_PSEPF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 Alternative name(s): PNP/PMP oxidase Short name=PNPOx Pyridoxal 5'-phosphate synthase | ||||
| Gene names |
| ||||
| Organism | Pseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 205922 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › ![]() |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity. HAMAP-Rule MF_01629 |
| Catalytic activity | Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule MF_01629 |
| Cofactor | Binds 1 FMN per subunit By similarity. |
| Pathway | Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP-Rule MF_01629 |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the pyridoxamine 5'-phosphate oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridoxine biosynthesis |
| Ligand | FMN Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: GOC pyridoxine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | FMN binding Inferred from electronic annotation. Source: HAMAP pyridoxamine-phosphate oxidase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 215 | 215 | Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629 | PRO_0000255876 | |||||
Regions | |||||||||
| Nucleotide binding | 79 – 80 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 143 – 144 | 2 | FMN By similarity | ||||||
| Region | 9 – 12 | 4 | Substrate binding By similarity | ||||||
| Region | 194 – 196 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 64 | 1 | FMN By similarity | ||||||
| Binding site | 67 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 69 | 1 | Substrate By similarity | ||||||
| Binding site | 86 | 1 | FMN By similarity | ||||||
| Binding site | 126 | 1 | Substrate By similarity | ||||||
| Binding site | 130 | 1 | Substrate By similarity | ||||||
| Binding site | 134 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genomic and genetic analyses of diversity and plant interactions of Pseudomonas fluorescens." Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., Harris S., Challis G.L., Yaxley A.M., Harris D. Thomson N.R.Genome Biol. 10:R51.1-R51.16(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pf0-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000094 Genomic DNA. Translation: ABA72972.1. |
| RefSeq | YP_346961.1. NC_007492.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2A2J based on UniProtKB P65682. |
| ProteinModelPortal | Q3KGY4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 205922.Pfl01_1229. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABA72972; ABA72972; Pfl01_1229. |
| GeneID | 3717078. |
| KEGG | pfo:Pfl01_1229. |
| PATRIC | 19884551. VBIPseFlu44242_1250. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0259. |
| HOGENOM | HOG000242755. |
| KO | K00275. |
| OMA | ERIEFWQ. |
| ProtClustDB | PRK05679. |
Enzyme and pathway databases | |
| BioCyc | PFLU205922:GJBD-1250-MONOMER. |
| UniPathway | UPA00190; UER00304. UPA00190; UER00305. |
Family and domain databases | |
| Gene3D | 2.30.110.10. 1 hit. |
| HAMAP | MF_01629. PdxH. |
| InterPro | IPR000659. Pyridox_Oxase. IPR019740. Pyridox_Oxase_CS. IPR011576. Pyridox_Oxase_FMN-bd. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN-bd. [Graphical view] |
| PANTHER | PTHR10851. PTHR10851. 1 hit. |
| Pfam | PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000190. Pyd_amn-ph_oxd. 1 hit. |
| SUPFAM | SSF50475. FMN_binding. 1 hit. |
| TIGRFAMs | TIGR00558. pdxH. 1 hit. |
| PROSITE | PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDXH_PSEPF | ||||||||
| Accession | Primary (citable) accession number: Q3KGY4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
