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B0KUA9 (PDXH_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:PputGB1_4286
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length215 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 – 215215Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000088116

Regions

Nucleotide binding79 – 802FMN By similarity
Nucleotide binding143 – 1442FMN By similarity
Region9 – 124Substrate binding 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
B0KUA9 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: AECAC5B72CABDE60

FASTA21524,586
        10         20         30         40         50         60 
MTQSLADMRR DYTRDGLAEA QAPGEPFVLF HQWFADAVKT EQAPVEANAM TLATVDGEGR 

        70         80         90        100        110        120 
PHCRVLLLKG LDEQGFTFFT NYESAKGQQL QANPFAAMTF FWPALERQVR IEGRVEKVSA 

       130        140        150        160        170        180 
QESDAYYQVR PLGSRLGAWA SPQSRVIAGR EELEGLVKAT EARFSDTQPH CPEHWGGYRL 

       190        200        210 
LPERIEFWQG RASRLHDRLN YRFVNGQWQR ERLAP 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABZ00175.1.
RefSeqYP_001670510.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KUA9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_4286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ00175; ABZ00175; PputGB1_4286.
GeneID5872093.
KEGGppg:PputGB1_4286.
PATRIC19935647. VBIPsePut76638_4289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-4363-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_PSEPG
AccessionPrimary (citable) accession number: B0KUA9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 43 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