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Q73G09 (PDXH_WOLPM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. 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:WD_1159
OrganismWolbachia pipientis wMel [Complete proteome] [HAMAP]
Taxonomic identifier163164 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length216 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 – 216216Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167771

Regions

Nucleotide binding79 – 802FMN By similarity
Nucleotide binding143 – 1442FMN 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
Q73G09 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 64F83515D339E8FC

FASTA21625,349
        10         20         30         40         50         60 
MAVALIFATR ARIKILFFDM IFSLEKDPFD LFSKWYKAVL NSPCEQPTAM TLATCSKDCI 

        70         80         90        100        110        120 
PSARVVLLKE YSKEGFVFFT NVNSKKGKEL TENPKAALVF HWIEFARQVR IEGEVKLLND 

       130        140        150        160        170        180 
ERTDKYFSSR ALGSQISAWC SKQSSILKDW QDFEQAIKLK EKEFHNTQVS RPDFWVGFCV 

       190        200        210 
IPKVIEFWQE GEYRKHIRFR YTLVEGSDWK VEQLYP 

« Hide

References

[1]"Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements."
Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F., Nelson W.C. expand/collapse author list , Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.
PLoS Biol. 2:327-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017196 Genomic DNA. Translation: AAS14809.1.
RefSeqNP_966875.1. NC_002978.6.

3D structure databases

ProteinModelPortalQ73G09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING163164.WD1159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS14809; AAS14809; WD_1159.
GeneID2738028.
KEGGwol:WD1159.
PATRIC24030917. VBIWolEnd21207_1148.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK749254.

Enzyme and pathway databases

BioCycWEND163164:GJ8W-1144-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_WOLPM
AccessionPrimary (citable) accession number: Q73G09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 77 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