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Q7N3W5 (PDXH_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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:plu2597
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length217 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 – 217217Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167732

Regions

Nucleotide binding81 – 822FMN By similarity
Nucleotide binding145 – 1462FMN By similarity
Region13 – 164Substrate binding By similarity
Region196 – 1983Substrate binding By similarity

Sites

Binding site661FMN By similarity
Binding site691FMN; via amide nitrogen By similarity
Binding site711Substrate By similarity
Binding site881FMN By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity
Binding site1361Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N3W5 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D4468E0B0F45DCFF

FASTA21725,233
        10         20         30         40         50         60 
MSEHNEFDVA ELRREYIRGG LRRKDLTEEP IELFERWLNQ ACNAKLSDPT AMSIATVDEN 

        70         80         90        100        110        120 
GQPYQRIVLL KHFDSNSLIF YTNLGSRKAK HLAHNNKISL HFPWYPLERQ VSFLGKAERL 

       130        140        150        160        170        180 
SPVEVVKYFH SRPRDSQIAA WASQQSSRIS ARGVLEGKFL ELKQKFLNGE VPLPSFWGGF 

       190        200        210 
KVTFDSVEFW QGGANRLHDR FIYQRQGDSW HVDRLAP 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571867 Genomic DNA. Translation: CAE14971.1.
RefSeqNP_929832.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N3W5.
SMRQ7N3W5. Positions 9-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu2597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE14971; CAE14971; plu2597.
GeneID2802603.
KEGGplu:plu2597.
PATRIC20509395. VBIPhoLum48522_2936.

Organism-specific databases

GenoListplu2597.
CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

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_PHOLL
AccessionPrimary (citable) accession number: Q7N3W5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 74 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