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P21159 (PDXH_MYXXA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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
Synonyms:fprA
OrganismMyxococcus xanthus
Taxonomic identifier34 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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.

Sequence caution

The sequence AAA25392.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
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 – 220220Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167724

Regions

Nucleotide binding84 – 852FMN By similarity
Nucleotide binding148 – 1492FMN By similarity
Region199 – 2013Substrate binding By similarity

Sites

Binding site691FMN By similarity
Binding site721FMN; via amide nitrogen By similarity
Binding site741Substrate By similarity
Binding site911FMN By similarity
Binding site1311Substrate By similarity
Binding site1351Substrate By similarity
Binding site1391Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P21159 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 656A388822028C2D

FASTA22025,285
        10         20         30         40         50         60 
MRTLTCVPDE STAKVHTCRA PFMLHRVMIP PDPIQRFAEL FERAKQAIAV DPNAMVVATV 

        70         80         90        100        110        120 
GDDGRPSARV VLLKDFDARG FVFYTNHESR KGREARAHPY AALCFYWQPL NEQVRVEGRV 

       130        140        150        160        170        180 
ERVTDAEADA YFQSRARGSQ VGAWASLQSQ PLATREELEA RVAEVEQKYA GQPVPRPPHW 

       190        200        210        220 
SGFRVVPDRI EFWHAQESRL HDRHVYLRED GGWRTQMLYP 

« Hide

References

[1]"Nucleotide sequence and transcriptional products of the csg locus of Myxococcus xanthus."
Hagen T.J., Shimkets L.J.
J. Bacteriol. 172:15-23(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Myxococcus xanthus FprA protein causes increased flavin biosynthesis in Escherichia coli."
Shimkets L.J.
J. Bacteriol. 172:24-30(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FMN-BINDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27429 Genomic DNA. Translation: AAA25392.2. Different initiation.
PIRS36092.
T10126.

3D structure databases

ProteinModelPortalP21159.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_MYXXA
AccessionPrimary (citable) accession number: P21159
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 89 of the entry and version 2 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