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Q0S6R1 (PDXH_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:RHA1_ro04994
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

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.

Sequence caution

The sequence ABG96775.1 differs from that shown. Reason: Erroneous initiation.

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 – 223223Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000255882

Regions

Nucleotide binding86 – 872FMN By similarity
Nucleotide binding150 – 1512FMN By similarity
Region9 – 124Substrate binding By similarity
Region202 – 2043Substrate binding By similarity

Sites

Binding site711FMN By similarity
Binding site741FMN; via amide nitrogen By similarity
Binding site761Substrate By similarity
Binding site931FMN By similarity
Binding site1331Substrate By similarity
Binding site1371Substrate By similarity
Binding site1411Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0S6R1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: BEC63647F464E792

FASTA22324,801
        10         20         30         40         50         60 
MNKDLAAMRV GYAHQGADGR YVDSDLDADQ LIGGWLPLMR LWLEDAVEAG VPEPNAMTLG 

        70         80         90        100        110        120 
TVDEHGHPCT RTVLCKGLST DGVLFFTNYD SDKGRQLEAV PYASVTFTWV PVARQITVRG 

       130        140        150        160        170        180 
PVERVSAEVT DEYWHSRPRG SRLGAWASEQ SKPIGSRAEL DAALLHAAER FPVDVDIPVR 

       190        200        210        220 
PDWGGILIRP AVVEFWQGRA NRMHNRIRTS LVDGSWTVER LQP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000431 Genomic DNA. Translation: ABG96775.1. Different initiation.
RefSeqYP_704933.1. NC_008268.1.

3D structure databases

ProteinModelPortalQ0S6R1.
SMRQ0S6R1. Positions 21-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro04994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG96775; ABG96775; RHA1_ro04994.
GeneID4222545.
KEGGrha:RHA1_ro04994.
PATRIC23208933. VBIRhoJos26306_5046.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-4991-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_RHOSR
AccessionPrimary (citable) accession number: Q0S6R1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 14, 2014
This is version 58 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