Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q28PH0 (PDXH_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:Jann_2475
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length206 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 – 206206Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292298

Regions

Nucleotide binding69 – 702FMN By similarity
Nucleotide binding133 – 1342FMN By similarity
Region183 – 1853Substrate binding By similarity

Sites

Binding site491FMN By similarity
Binding site521FMN; via amide nitrogen By similarity
Binding site541Substrate By similarity
Binding site761FMN By similarity
Binding site1161Substrate By similarity
Binding site1201Substrate By similarity
Binding site1241Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28PH0 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: AC4D055EB3CF4836

FASTA20622,671
        10         20         30         40         50         60 
MSERSGIFAG DDPFVLARAW LAEAEASEPN DPNAIALSTV DADGLPNARM VLLKEIESHG 

        70         80         90        100        110        120 
AGQGGFVFYT NYGSAKGQEI AQAGKAAFVC HWKSLHRQIR VRGLTETEDG PQADAYYASR 

       130        140        150        160        170        180 
SLKSRLGAWA SDQSKPLSSR GALMADVARV TAEQGTNPKR PPFWGGVRIT PLEIEFWADG 

       190        200 
AFRLHDRFQW RRGSVDDPWE VQRLNP 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD55392.1.
RefSeqYP_510417.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28PH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290400.Jann_2475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD55392; ABD55392; Jann_2475.
GeneID3934933.
KEGGjan:Jann_2475.
PATRIC22148734. VBIJanSp43325_2629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK933776.

Enzyme and pathway databases

BioCycJSP290400:GI1R-2497-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_JANSC
AccessionPrimary (citable) accession number: Q28PH0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 59 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