Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7VP83 (PDXH_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:HD_0214
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length209 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 – 209209Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167710

Regions

Nucleotide binding74 – 752FMN By similarity
Nucleotide binding138 – 1392FMN By similarity
Region7 – 104Substrate binding By similarity

Sites

Binding site591FMN By similarity
Binding site621FMN; via amide nitrogen By similarity
Binding site641Substrate By similarity
Binding site811FMN By similarity
Binding site1211Substrate By similarity
Binding site1251Substrate By similarity
Binding site1291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VP83 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 6BB1A74F3A39D8AF

FASTA20924,165
        10         20         30         40         50         60 
MDLHNIRADY TKQQLSKKEC DANPMKQFER WLNEAIMAKV NEPTAMNMAT VIDGKPTSRI 

        70         80         90        100        110        120 
VLLKEVDQQG FIFFTNYQSC KGWAIALNPY VALTFFWPEL ERSVRVEGIA TKLSEQASDD 

       130        140        150        160        170        180 
YFASRPYASR IGAWASDQSQ VLSSKRTLVA KVALLSAKYP LFVPRPAHWG GYLVQPTKIE 

       190        200 
FWQGRPSWLH DRICYWLVEN EWLKERLSP 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP95204.1.
RefSeqNP_872815.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VP83.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD0214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP95204; AAP95204; HD_0214.
GeneID1490221.
KEGGhdu:HD0214.
PATRIC20177005. VBIHaeDuc133973_0171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-199-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_HAEDU
AccessionPrimary (citable) accession number: Q7VP83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 77 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