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Q2N6B2 (PDXH_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ELI_13435
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter ›

Protein attributes

Sequence length212 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.

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.

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292291

Regions

Nucleotide binding72 – 732FMN By similarity
Nucleotide binding136 – 1372FMN By similarity
Region187 – 1893Substrate binding By similarity

Sites

Binding site571FMN By similarity
Binding site601FMN; via amide nitrogen By similarity
Binding site621Substrate By similarity
Binding site791FMN By similarity
Binding site1191Substrate By similarity
Binding site1231Substrate By similarity
Binding site1271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N6B2 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 49CA376F719EFAB0

FASTA21224,124
        10         20         30         40         50         60 
MQSEESIMTD LATSEIPETD PFALFAEWME EARASELNDP NAMALATATP DGAPSVRMVL 

        70         80         90        100        110        120 
LKDHGPQGFT FYTNAESRKG EEIRANAQTA LLFHWKSLRR QIRVEGPVRE VAPEVADAYF 

       130        140        150        160        170        180 
HSRARESQLG AVASDQSRPL EDRRVFVDRF RAAQERFDEG EVERPAYWTG FTVTPQRIEF 

       190        200        210 
WCDRPNRLHD RRLFTLSGAG DALSWTSTLL YP

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000157 Genomic DNA. Translation: ABC64779.1.
RefSeqYP_459576.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N6B2.
ModBaseSearch...

Protein-protein interaction databases

STRING314225.ELI_13435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC64779; ABC64779; ELI_13435.
GeneID3871010.
KEGGeli:ELI_13435.
PATRIC21862541. VBIEryLit102657_2683.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAHWSGFRI.

Enzyme and pathway databases

BioCycELIT314225:GHLE-2732-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. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_ERYLH
AccessionPrimary (citable) accession number: Q2N6B2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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