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Q9K3V7 (PDXH_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:SCO4387
ORF Names:SCD10.19c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length234 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 – 234234Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167761

Regions

Nucleotide binding96 – 972FMN By similarity
Nucleotide binding160 – 1612FMN By similarity
Region27 – 304Substrate binding By similarity
Region212 – 2143Substrate binding By similarity

Sites

Binding site811FMN By similarity
Binding site841FMN; via amide nitrogen By similarity
Binding site861Substrate By similarity
Binding site1031FMN By similarity
Binding site1431Substrate By similarity
Binding site1471Substrate By similarity
Binding site1511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K3V7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 144580483B5366FB

FASTA23426,012
        10         20         30         40         50         60 
MGGVTDRDAD SAVPTADPVP FDLASMRKQY RAEGLSETEL AATPVEQFAR WFKQAATDGG 

        70         80         90        100        110        120 
LFEPNAMVVS TADPEGRPSS RTVLLKHFDE QGFVFYTNYD SRKARELDAN PHVSLLFPWH 

       130        140        150        160        170        180 
PMARQVVVTG VARRTGRDET AAYFRTRPHG SQLGAWASVQ SSVVADRRAL DGAYAELAAR 

       190        200        210        220        230 
YPEGEQVPVP PHWGGFRVVP DAVEFWQGRE NRLHDRLRYV AEGGGGWRVE RLSP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939119 Genomic DNA. Translation: CAB95898.1.
RefSeqNP_628556.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9K3V7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO4387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB95898; CAB95898; CAB95898.
GeneID1099827.
KEGGsco:SCO4387.
PATRIC23738582. VBIStrCoe124346_4455.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.
PhylomeDBQ9K3V7.

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_STRCO
AccessionPrimary (citable) accession number: Q9K3V7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 81 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