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Q0RUF3 (PDXH_FRAAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:pdxH
Ordered Locus Names:FRAAL0106
OrganismFrankia alni (strain ACN14a) [Complete proteome] [HAMAP]
Taxonomic identifier326424 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceInferred 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

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292293

Regions

Nucleotide binding102 – 1032FMN By similarity
Nucleotide binding166 – 1672FMN By similarity
Region32 – 354Substrate binding By similarity
Region218 – 2203Substrate binding By similarity

Sites

Binding site871FMN By similarity
Binding site901FMN; via amide nitrogen By similarity
Binding site921Substrate By similarity
Binding site1091FMN By similarity
Binding site1491Substrate By similarity
Binding site1531Substrate By similarity
Binding site1571Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0RUF3 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 33E1DC55280D0BC3

FASTA24126,590
        10         20         30         40         50         60 
MASNPPSAAS PRRTAVSPGA DRPDGPDPAG QRQSYHAGRL EPEQLATTWV EQFARWFADA 

        70         80         90        100        110        120 
STAGAGVPEA NAAVFATASA DGRPSARTVL LKGFDHRGFV IYTNYTSRKG RESAENPFGS 

       130        140        150        160        170        180 
LVFPWYTLER QVVAIGAVER VSRTETEQYF ASRPRGSQLG AWASHQSQII ESRDVLDARA 

       190        200        210        220        230        240 
AELAARWPAG TPVPTPPFWG GLRLVPDTVE FWQGRTNRLH DRLRYRRVCT ADRWAVERLS 


P 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573213 Genomic DNA. Translation: CAJ58788.1.
RefSeqYP_710403.1. NC_008278.1.

3D structure databases

ProteinModelPortalQ0RUF3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326424.FRAAL0106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4236957.
KEGGfal:FRAAL0106.
PATRIC21910231. VBIFraAln347_0089.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMARKWIDDA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycFALN326424:GJ82-105-MONOMER.
UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_FRAAA
AccessionPrimary (citable) accession number: Q0RUF3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways