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Q87DU7 (PDXH_XYLFT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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:PD_0583
OrganismXylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]
Taxonomic identifier183190 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length208 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 – 208208Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167778

Regions

Nucleotide binding68 – 692FMN By similarity
Nucleotide binding135 – 1362FMN By similarity
Region186 – 1883Substrate binding By similarity

Sites

Binding site531FMN By similarity
Binding site561FMN; via amide nitrogen By similarity
Binding site581Substrate By similarity
Binding site751FMN By similarity
Binding site1181Substrate By similarity
Binding site1221Substrate By similarity
Binding site1261Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87DU7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5A037D8DC43FE233

FASTA20823,810
        10         20         30         40         50         60 
MIFPCLFQSM LNLYAEALST FSLLFEEAKS SSEIEPDAMM LATASLEGHP SVRTVLLKKF 

        70         80         90        100        110        120 
DARGFVFYSH LDSPKGRDLQ ANPQAALLFL WRSLREAGVQ VRIEGRVQQV LAEEADAYFA 

       130        140        150        160        170        180 
SRPRQSQIGA WASMQSCPLG SPEEFQARLA EVKAMFEGRD VPRPEEWVGF RVVPQVFEFW 

       190        200 
YGASFRLHER WRYQADAAGY WRKSLLYP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009442 Genomic DNA. Translation: AAO28456.1.
RefSeqNP_778807.1. NC_004556.1.

3D structure databases

ProteinModelPortalQ87DU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING183190.PD0583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO28456; AAO28456; PD_0583.
GeneID1144786.
KEGGxft:PD0583.
PATRIC24148891. VBIXylFas71109_0761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycXFAS183190:GIX4-583-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_XYLFT
AccessionPrimary (citable) accession number: Q87DU7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 75 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