Reviewed,
UniProtKB/Swiss-Prot Q7VU72 (PDXH_BORPE)
Last modified
February 9, 2010.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 | Bordetella pertussis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 520 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 210 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 MF_01629 |
| Catalytic activity | Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629 |
| Cofactor | Binds 1 FMN per subunit By similarity. HAMAP MF_01629 |
| Pathway | Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629 |
| Subunit structure | Homodimer By similarity. HAMAP 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 |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 – 210 | 210 | Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629 | PRO_0000167691 | |||||
Regions | |||||||||
| Nucleotide binding | 75 – 76 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 139 – 140 | 2 | FMN By similarity | ||||||
| Region | 7 – 10 | 4 | Substrate binding By similarity | ||||||
| Region | 188 – 190 | 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] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640420 Genomic DNA. Translation: CAE43518.1. |
| RefSeq | NP_881799.1. |
3D structure databases | |
| SMR | Q7VU72. Positions 13-210. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2667670. |
| KEGG | bpe:BP3251. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG327559. |
| OMA | FTFFTNY. |
| PhylomeDB | Q7VU72. |
Enzyme and pathway databases | |
| BioCyc | BPER257313:BP3251-MONOMER. |
| BRENDA | 1.4.3.5. 21511. |
Family and domain databases | |
| HAMAP | MF_01629. PdxH. [Tree] |
| InterPro | IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR009002. Split_barrel_FMN-bd_related. IPR012349. Split_barrel_FMN_bd. [Graphical view] |
| Gene3D | G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit. |
| PANTHER | PTHR10851. Pyridox_oxidase. 1 hit. |
| Pfam | PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00558. pdxH. 1 hit. |
| PROSITE | PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDXH_BORPE | ||||||||
| Accession | Primary (citable) accession number: Q7VU72 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


