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Q7UKQ9 (PDXH_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:RB10006
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length223 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 – 223223Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167748

Regions

Nucleotide binding83 – 842FMN By similarity
Nucleotide binding147 – 1482FMN By similarity
Region13 – 164Substrate binding By similarity
Region199 – 2013Substrate binding By similarity

Sites

Binding site681FMN By similarity
Binding site711FMN; via amide nitrogen By similarity
Binding site731Substrate By similarity
Binding site901FMN By similarity
Binding site1301Substrate By similarity
Binding site1341Substrate By similarity
Binding site1381Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UKQ9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E89AF484C5C18F6B

FASTA22325,677
        10         20         30         40         50         60 
MSDFIPPAMD QMRKNYSLGG LHENDAKSDP LVQFQSWFEE ALEDVPNWFE PNAMTLSTSD 

        70         80         90        100        110        120 
VSGDITSRIV LLKGVEEKKF LFYTNYDSTK GSQMRANPRV SLCLFWPHCQ RQVRIQGTVD 

       130        140        150        160        170        180 
KVSREMSETY FHSRPRDSQL GAHVSQQSSV IDSREAMESS LAQLKARYPE GTQIPLPENW 

       190        200        210        220 
GGYAVTPMSF EFWQGRPSRL HDRLVYKRDD ADSNDWVMQR LSP 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294150 Genomic DNA. Translation: CAD76573.1.
RefSeqNP_869187.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UKQ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB10006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD76573; CAD76573; RB10006.
GeneID1796073.
KEGGrba:RB10006.
PATRIC23251119. VBIRhoBal59814_4819.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

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_RHOBA
AccessionPrimary (citable) accession number: Q7UKQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 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