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Q9JTZ1 (PDXH_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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:NMA1572
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [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_0000167726

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
Q9JTZ1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6FA480903939ED5C

FASTA21024,201
        10         20         30         40         50         60 
MDLHNIREDY SKRELSEGDC ADNPIEQFER WLDEAVRAQV NEPTAVNVAA VDGRGRPNSR 

        70         80         90        100        110        120 
MVLLKEVNSE GFVFFTNYHS RKGRSLDAHP FAAMTFFWPE LERQVRVEGR VERLAEKLSD 

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

       190        200        210 
EFWQGRPSRL HDRIQYRLLD GGWIRERLSP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM08717.1.
PIRG81849.
RefSeqYP_002342889.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JTZ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA1572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM08717; CAM08717; NMA1572.
GeneID907960.
KEGGnma:NMA1572.
PATRIC20364234. VBINeiMen132687_1821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1431-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_NEIMA
AccessionPrimary (citable) accession number: Q9JTZ1
Secondary accession number(s): A1ISG1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 84 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