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A5FB76 (PDXH_FLAJ1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:Fjoh_4542
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

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_0000335784

Regions

Nucleotide binding77 – 782FMN By similarity
Nucleotide binding141 – 1422FMN By similarity
Region8 – 114Substrate 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
A5FB76 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 7A433F3EB79D4BC6

FASTA21424,671
        10         20         30         40         50         60 
MNDLSNYRKS YEKSELLETN IPEDPINLFN RWFHEVEDFG GSGEVNAMTV STIGLDGFPK 

        70         80         90        100        110        120 
SRVVLLKKFS EEGFIFYTNY NSEKGKAIEA NPNVCLSFFW QEAERQVIIK GIAQKTSEII 

       130        140        150        160        170        180 
SDNYFDSRPD GSKLGAIVSH QSEVIPSRTF LEENLKKLEA EFEGKPIPRP ENWGGYLVTP 

       190        200        210 
LQVEFWQGRP NRLHDRIRYT SQSDFSWTIE RLSS 

« Hide

References

[1]"Complete sequence of Flavobacterium johnsoniae UW101."
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., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000685 Genomic DNA. Translation: ABQ07541.1.
RefSeqYP_001196860.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FB76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING376686.Fjoh_4542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ07541; ABQ07541; Fjoh_4542.
GeneID5092615.
KEGGfjo:Fjoh_4542.
PATRIC21903719. VBIFlaJoh53613_4697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBCLSK851562.

Enzyme and pathway databases

BioCycFJOH376686:GIXN-4614-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_FLAJ1
AccessionPrimary (citable) accession number: A5FB76
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 55 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