Q8XS03 (PDXH2_RALSO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 76.
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 2 EC=1.4.3.5 Alternative name(s): PNP/PMP oxidase 2 Short name=PNPOx 2 Pyridoxal 5'-phosphate synthase 2 | ||||||
| Gene names |
| ||||||
| Encoded on | Plasmid megaplasmid Rsp | ||||||
| Organism | Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 267608 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia › ![]() |
Protein attributes
| Sequence length | 213 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. HAMAP-Rule MF_01629 |
| 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. HAMAP-Rule MF_01629 |
| 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 Plasmid |
| 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 – 213 | 213 | Pyridoxine/pyridoxamine 5'-phosphate oxidase 2 HAMAP-Rule MF_01629 | PRO_0000167745 | |||||
Regions | |||||||||
| Nucleotide binding | 75 – 76 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 139 – 140 | 2 | FMN By similarity | ||||||
| Region | 190 – 192 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 60 | 1 | FMN By similarity | ||||||
| Binding site | 63 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 65 | 1 | Substrate By similarity | ||||||
| Binding site | 82 | 1 | FMN By similarity | ||||||
| Binding site | 122 | 1 | Substrate By similarity | ||||||
| Binding site | 126 | 1 | Substrate By similarity | ||||||
| Binding site | 130 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the plant pathogen Ralstonia solanacearum." Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., Moisan A. Boucher C.A.Nature 415:497-502(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GMI1000. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL646053 Genomic DNA. Translation: CAD17829.1. |
| RefSeq | NP_522239.1. NC_003296.1. |
3D structure databases | |
| ProteinModelPortal | Q8XS03. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 267608.RSp0678. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAD17829; CAD17829; RSp0678. |
| GeneID | 1222985. |
| KEGG | rso:RSp0678. |
| PATRIC | 20266959. VBIRalSol70888_4151. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0259. |
| HOGENOM | HOG000242755. |
| KO | K00275. |
| OMA | INDANAM. |
| ProtClustDB | PRK05679. |
Enzyme and pathway databases | |
| BioCyc | RSOL267608:GCVU-4182-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 | PDXH2_RALSO | ||||||||
| Accession | Primary (citable) accession number: Q8XS03 | ||||||||
| 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
