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B9JAN3 (PDXH_AGRRK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:Arad_1220
OrganismAgrobacterium radiobacter (strain K84 / ATCC BAA-868) [Complete proteome] [HAMAP]
Taxonomic identifier311403 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

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_1000186285

Regions

Nucleotide binding68 – 692FMN By similarity
Nucleotide binding132 – 1332FMN By similarity
Region183 – 1853Substrate binding By similarity

Sites

Binding site531FMN By similarity
Binding site561FMN; via amide nitrogen By similarity
Binding site581Substrate By similarity
Binding site751FMN By similarity
Binding site1151Substrate By similarity
Binding site1191Substrate By similarity
Binding site1231Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B9JAN3 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: A7C543A00B6ACD94

FASTA20623,898
        10         20         30         40         50         60 
MSENELTSGD FTEQNEPFAL FAAWLREAEA TEPNDPNAVA LATVDKDGLP NVRMVLLKGF 

        70         80         90        100        110        120 
DSQGFVFYTN FESQKGQEIL SQKKAAMCFH WKSLRRQVRL RGLVEVVSDK EADEYYKTRA 

       130        140        150        160        170        180 
RGSRIGAWAS KQSRPLEGRF ALEKAVAEYT ARYALGDIPR PPHWSGFRIR PLSIEFWHDR 

       190        200 
PFRLHDRVEF RREVPEGAWE KVRMYP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000628 Genomic DNA. Translation: ACM25716.1.
RefSeqYP_002543642.1. NC_011985.1.

3D structure databases

ProteinModelPortalB9JAN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING311403.Arad_1220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM25716; ACM25716; Arad_1220.
GeneID7371219.
KEGGara:Arad_1220.
PATRIC20802622. VBIAgrRad129173_3418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAAVLHWKS.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycARAD311403:GHU8-942-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_AGRRK
AccessionPrimary (citable) accession number: B9JAN3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 38 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