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B9JSN3 (PDXH_AGRVS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:Avi_1026
OrganismAgrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain S4)) [Complete proteome] [HAMAP]
Taxonomic identifier311402 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

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_1000186286

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
B9JSN3 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: C5F1F4F1EF76492C

FASTA20623,781
        10         20         30         40         50         60 
MSQNELTTGD FTDEHEPFGL FETWLTEAKA SEINDPNAVA LATVDESGLP NVRMVLLKDF 

        70         80         90        100        110        120 
DQNGFVFYTN FESQKGTEIL SQKKAAMCFH WKSLRRQVRL RGEVEVVSDA EADAYYQTRP 

       130        140        150        160        170        180 
IGSRIGAWAS KQSRPLESRF ALEKAVAEYT ARYALGSIPR PAHWSGFRIK PLTIEFWRDG 

       190        200 
KFRLHDRIEF RREALGQPWN KVRMYP 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000633 Genomic DNA. Translation: ACM35726.1.
RefSeqYP_002548732.1. NC_011989.1.

3D structure databases

ProteinModelPortalB9JSN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING311402.Avi_1026.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM35726; ACM35726; Avi_1026.
GeneID7387116.
KEGGavi:Avi_1026.
PATRIC20826756. VBIAgrVit37146_3052.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMASIEFWCD.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycAVIT311402:GH2Y-785-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_AGRVS
AccessionPrimary (citable) accession number: B9JSN3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 39 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