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B4THC5 (PDXH_SALHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SeHA_C1618
OrganismSalmonella heidelberg (strain SL476) [Complete proteome] [HAMAP]
Taxonomic identifier454169 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length218 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.

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.

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000186336

Regions

Nucleotide binding82 – 832FMN By similarity
Nucleotide binding146 – 1472FMN By similarity
Region14 – 174Substrate binding By similarity
Region197 – 1993Substrate binding By similarity

Sites

Binding site671FMN By similarity
Binding site701FMN; via amide nitrogen By similarity
Binding site721Substrate By similarity
Binding site891FMN By similarity
Binding site1291Substrate By similarity
Binding site1331Substrate By similarity
Binding site1371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4THC5 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 43CAF2F67B6BFB70

FASTA21825,499
        10         20         30         40         50         60 
MSDNDQLQQI AHLRREYTKG GLRRRDLPAE PLTLFERWLG QACDARLADP TAMVVATVDD 

        70         80         90        100        110        120 
KGQPYQRIVL LKHYDEKGLV FYTNLGSRKA HQIEHNPRIS LLFPWHMLER QVMVTGKAER 

       130        140        150        160        170        180 
LSTLEVVRYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSIEQMEF WQGGEHRLHD RFLYQRDDGA WKIDRLAP

« Hide

References

[1]"Complete genome of Salmonella heidelberg strain SL476."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SL476.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001120 Genomic DNA. Translation: ACF68228.1.
RefSeqYP_002045486.1. NC_011083.1.

3D structure databases

ProteinModelPortalB4THC5.
SMRB4THC5. Positions 5-218.
ModBaseSearch...

Protein-protein interaction databases

STRING454169.SeHA_C1618.

Proteomic databases

PRIDEB4THC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF68228; ACF68228; SeHA_C1618.
GeneID6490815.
KEGGseh:SeHA_C1618.
PATRIC18510934. VBISalEnt43179_1574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAERIEFWQ.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycSENT454169:GHYG-2488-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. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_SALHS
AccessionPrimary (citable) accession number: B4THC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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