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B2IX27 (PDXH_NOSP7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. 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:Npun_F6283
OrganismNostoc punctiforme (strain ATCC 29133 / PCC 73102) [Complete proteome] [HAMAP]
Taxonomic identifier63737 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length214 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 – 214214Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000186322

Regions

Nucleotide binding77 – 782FMN By similarity
Nucleotide binding141 – 1422FMN By similarity
Region9 – 124Substrate binding By similarity
Region192 – 1943Substrate binding By similarity

Sites

Binding site621FMN By similarity
Binding site651FMN; via amide nitrogen By similarity
Binding site671Substrate By similarity
Binding site841FMN By similarity
Binding site1241Substrate By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2IX27 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 6DCE87A7521DC1CF

FASTA21425,038
        10         20         30         40         50         60 
MDKTVADLRK DYTLEGLSEL EVDLNPFIQF KKWFDQALAG QLPEPNAMTL ATVTPDGKPS 

        70         80         90        100        110        120 
ARMVLLKDFD ERGFAFFTNY NSRKGQELAE NPLAALVFWW AELERQVRIC GYVEKVSETE 

       130        140        150        160        170        180 
SDQYFDTRPP NSRLGAWVSN QSEVIESREV LERRMQEFYS KYENQEIPRP PHWGGLRVIP 

       190        200        210 
TEIEFWQGRS SRLHDRLLYS RLDNGTWKID RLSP 

« Hide

References

[1]"Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C. expand/collapse author list , Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29133 / PCC 73102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001037 Genomic DNA. Translation: ACC84562.1.
RefSeqYP_001869505.1. NC_010628.1.

3D structure databases

ProteinModelPortalB2IX27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING63737.Npun_F6283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC84562; ACC84562; Npun_F6283.
GeneID6255630.
KEGGnpu:Npun_F6283.
PATRIC22766491. VBINosPun48114_7367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK895487.

Enzyme and pathway databases

BioCycNPUN63737:GJNP-6152-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_NOSP7
AccessionPrimary (citable) accession number: B2IX27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 42 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