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Q8ED71 (PDXH_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. 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:SO_2895
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length212 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
Reference 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 – 212212Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167754

Regions

Nucleotide binding76 – 772FMN By similarity
Nucleotide binding140 – 1412FMN By similarity
Region8 – 114Substrate binding By similarity
Region191 – 1933Substrate binding By similarity

Sites

Binding site611FMN By similarity
Binding site641FMN; via amide nitrogen By similarity
Binding site661Substrate By similarity
Binding site831FMN By similarity
Binding site1231Substrate By similarity
Binding site1271Substrate By similarity
Binding site1311Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ED71 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AB4EAE5E0D4EF757

FASTA21224,345
        10         20         30         40         50         60 
MTDLSDIRRE YTQGGLRRAD LPKNPMQLFE LWMTQARDAQ LSDPTAMCVA TVDEHGQPFQ 

        70         80         90        100        110        120 
RIVLLKRFDD SGFVFFTNLG SRKALQIAAN NKVSLHFPWH PIERQVSILG EAQPLSTAEV 

       130        140        150        160        170        180 
LKYFMTRPKE SQIAAWVSQQ SSKLSARQVL EGKFFEMKAK FAKGDVPLPS FWGGYLVKPS 

       190        200        210 
SIEFWQGGEH RLHDRFLYTR EAQAWQIDRL AP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN55911.1.
RefSeqNP_718467.1. NC_004347.2.

3D structure databases

ProteinModelPortalQ8ED71.
SMRQ8ED71. Positions 1-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_2895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN55911; AAN55911; SO_2895.
GeneID1170585.
KEGGson:SO_2895.
PATRIC23525432. VBISheOne101494_2793.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.
PhylomeDBQ8ED71.

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_SHEON
AccessionPrimary (citable) accession number: Q8ED71
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 80 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