Q9AJD6 (PNO_MICLT) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 52.
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 4-oxidase EC=1.1.3.12 | ||
| Gene names |
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| Organism | Microbacterium luteolum (Aureobacterium luteolum) | ||
| Taxonomic identifier | 69367 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Microbacterium |
Protein attributes
| Sequence length | 507 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Pyridoxine + O2 = pyridoxal + H2O2. |
| Cofactor | FAD. |
| Pathway | Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (oxidase route): step 1/1. |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the GMC oxidoreductase family. |
| Biophysicochemical properties | Kinetic parameters: KM=54.5 µM for pyridoxine Ref.1 KM=206.64 µM for oxygen KM=9.71 µM for 2,6-dichloroindophenol KM=50.16 µM for vitamin K3 pH dependence: Optimum pH is 7.5-8.0. Temperature dependence: Optimum temperature is 40 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | alcohol metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | choline dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro pyridoxine 4-oxidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Purification, molecular cloning, and characterization of pyridoxine 4-oxidase from Microbacterium." Kaneda Y., Ohnishi K., Yagi T. Biosci. Biotechnol. Biochem. 66:1022-1031(2002) [PubMed: 12092811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20 AND 348-364, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: YK-1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB049341 Genomic DNA. Translation: BAB39853.1. |
| PIR | JC7855. |
3D structure databases | |
| ProteinModelPortal | Q9AJD6. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR012132. GMC_OxRdtase. IPR000172. GMC_OxRdtase_N. IPR007867. GMC_OxRtase_C. [Graphical view] |
| Pfam | PF05199. GMC_oxred_C. 1 hit. PF00732. GMC_oxred_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000137. Alcohol_oxidase. 1 hit. |
| PROSITE | PS00623. GMC_OXRED_1. 1 hit. PS00624. GMC_OXRED_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PNO_MICLT | ||||||||
| Accession | Primary (citable) accession number: Q9AJD6 | ||||||||
| 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 |

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