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B4RM90 (PDXH_NEIG2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:NGK_1250
OrganismNeisseria gonorrhoeae (strain NCCP11945) [Complete proteome] [HAMAP]
Taxonomic identifier521006 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length210 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 – 210210Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000186320

Regions

Nucleotide binding75 – 762FMN By similarity
Nucleotide binding139 – 1402FMN By similarity
Region7 – 104Substrate binding By similarity
Region189 – 1913Substrate binding By similarity

Sites

Binding site601FMN By similarity
Binding site631FMN; via amide nitrogen By similarity
Binding site651Substrate By similarity
Binding site821FMN By similarity
Binding site1221Substrate By similarity
Binding site1261Substrate By similarity
Binding site1301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RM90 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: FF9C40DA2A1B5BB9

FASTA21024,177
        10         20         30         40         50         60 
MDLHNIREDY SKRELSEADC ADNPIEQFER WLDEAVRAEV NEPTAVNVAA VDGRGRPNSR 

        70         80         90        100        110        120 
MVLLKEVNSE GFVFFTNYHS RKGRSLELNP FAAMTFFWPE LERQVRVEGR VGRLAEKLSD 

       130        140        150        160        170        180 
EYFESRPYQS RLGAWASAQS EVIPNKAVLV AKAAAVGLKH PLHVPRPPHW GGYIVIPDLI 

       190        200        210 
EFWQGRPSRL HDRIQYRLLD GGWIRERLSP 

« Hide

References

[1]"Complete genome sequence of Neisseria gonorrhoeae NCCP11945."
Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCCP11945.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001050 Genomic DNA. Translation: ACF29926.1.
RefSeqYP_002001875.1. NC_011035.1.

3D structure databases

ProteinModelPortalB4RM90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521006.NGK_1250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF29926; ACF29926; NGK_1250.
GeneID6447413.
KEGGngk:NGK_1250.
PATRIC20340949. VBINeiGon87511_1339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycNGON521006:GJ73-1274-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_NEIG2
AccessionPrimary (citable) accession number: B4RM90
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 43 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