Q2GJ82 (PDXH_ANAPZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 57.
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 | Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 212042 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group › ![]() |
Protein attributes
| Sequence length | 206 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 – 206 | 206 | Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629 | PRO_0000255852 | |||||
Regions | |||||||||
| Nucleotide binding | 69 – 70 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 133 – 134 | 2 | FMN By similarity | ||||||
| Region | 184 – 186 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 54 | 1 | FMN By similarity | ||||||
| Binding site | 57 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 59 | 1 | Substrate By similarity | ||||||
| Binding site | 76 | 1 | FMN By similarity | ||||||
| Binding site | 116 | 1 | Substrate By similarity | ||||||
| Binding site | 120 | 1 | Substrate By similarity | ||||||
| Binding site | 124 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. Tettelin H.PLoS Genet. 2:208-222(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HZ. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000235 Genomic DNA. Translation: ABD44041.1. |
| RefSeq | YP_505569.1. NC_007797.1. |
3D structure databases | |
| ProteinModelPortal | Q2GJ82. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 212042.APH_1008. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABD44041; ABD44041; APH_1008. |
| GeneID | 3930979. |
| KEGG | aph:APH_1008. |
| PATRIC | 20950750. VBIAnaPha602_1076. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0259. |
| HOGENOM | HOG000242755. |
| KO | K00275. |
| OMA | ERIEFWQ. |
| ProtClustDB | CLSK747290. |
Enzyme and pathway databases | |
| BioCyc | APHA212042:GHPM-1016-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_ANAPZ | ||||||||
| Accession | Primary (citable) accession number: Q2GJ82 | ||||||||
| 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
