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Q2W8Y5 (PDXH_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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:amb0886
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length195 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.

Sequence caution

The sequence BAE49690.1 differs from that shown. Reason: Erroneous initiation.

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 – 195195Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000255870

Regions

Nucleotide binding59 – 602FMN By similarity
Nucleotide binding123 – 1242FMN By similarity
Region174 – 1763Substrate binding By similarity

Sites

Binding site441FMN By similarity
Binding site471FMN; via amide nitrogen By similarity
Binding site491Substrate By similarity
Binding site661FMN By similarity
Binding site1061Substrate By similarity
Binding site1101Substrate By similarity
Binding site1141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W8Y5 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 90C68EEC3EBF0D46

FASTA19522,263
        10         20         30         40         50         60 
MSAPEADPLV LFHKWMDEAE KAEPNDPNAM ALATADAEGR PSVRMVLLKG ADQDGFVFFT 

        70         80         90        100        110        120 
NLESRKGQEL AANPHAALCL HWKSLRRQIR VEGSITRVSD EEADAYFATR ARASQIGAWA 

       130        140        150        160        170        180 
SIQSRPLTGR FELEKRVGEF AAKFGLGKVP RPPHWSGFRL APRRIEFWHD RPFRLHDRFD 

       190 
YVRDGDGWHL EHLYP 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE49690.1. Different initiation.
RefSeqYP_420249.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W8Y5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb0886.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE49690; BAE49690; amb0886.
GeneID3803618.
KEGGmag:amb0886.
PATRIC22436073. VBIMagMag129836_0900.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANFESQKG.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-894-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_MAGSA
AccessionPrimary (citable) accession number: Q2W8Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: April 16, 2014
This is version 63 of the entry and version 2 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