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A5IH19 (PDXH_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:LPC_2766
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length215 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 – 215215Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000069695

Regions

Nucleotide binding79 – 802FMN By similarity
Nucleotide binding143 – 1442FMN By similarity
Region11 – 144Substrate binding By similarity
Region194 – 1963Substrate binding By similarity

Sites

Binding site641FMN By similarity
Binding site671FMN; via amide nitrogen By similarity
Binding site691Substrate By similarity
Binding site861FMN By similarity
Binding site1261Substrate By similarity
Binding site1301Substrate By similarity
Binding site1341Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IH19 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 86C5C8C6206BA2EC

FASTA21525,263
        10         20         30         40         50         60 
MSKFRSLADI RRDYGELQLS EESAENDPIS QFKLWFDDVL LNEKNDPTAM VLSTVDEKGY 

        70         80         90        100        110        120 
PDSRVVLLKG LENGNFIFYT NYQSAKAMQI QKNPYAALNF YWPQMARQVR VRGRVKKISS 

       130        140        150        160        170        180 
EQSDAYFSSR PLKSQFSAIV SPQSQEILDR ISLEDALNQL IEEYGQKPVV RPENWGGYMI 

       190        200        210 
IPDEIEFWQG RDNRLHDRIH YYRHGHEWTH RRLAP 

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000675 Genomic DNA. Translation: ABQ56669.1.
RefSeqYP_001252015.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5IH19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400673.LPC_2766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ56669; ABQ56669; LPC_2766.
GeneID5182545.
KEGGlpc:LPC_2766.
PATRIC22312119. VBILegPne45588_2864.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK832243.

Enzyme and pathway databases

BioCycLPNE400673:GCIT-645-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_LEGPC
AccessionPrimary (citable) accession number: A5IH19
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 50 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