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Q0ARD7 (PDXH_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:Mmar10_0857
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length222 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 – 222222Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292301

Regions

Nucleotide binding84 – 852FMN By similarity
Nucleotide binding148 – 1492FMN By similarity
Region199 – 2013Substrate binding By similarity

Sites

Binding site691FMN By similarity
Binding site721FMN; via amide nitrogen By similarity
Binding site741Substrate By similarity
Binding site911FMN By similarity
Binding site1311Substrate By similarity
Binding site1351Substrate By similarity
Binding site1391Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ARD7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 1381D59AEF7C630B

FASTA22224,863
        10         20         30         40         50         60 
MSDDKLIPAT PDADAYAKTA DANAAEIFDR DEPFALFADW LTEAKKKEPN DANAMALATA 

        70         80         90        100        110        120 
DASGLPDVRM VLLKDVDADG FVFYTNLESG KGGQLADNPQ AALCFHWKSL RRQVRVRGAV 

       130        140        150        160        170        180 
EPVSAGEADA YFASRARDSR IGAWASKQSR PLESRFALEK SVAREAARFG LGEVPRPPHW 

       190        200        210        220 
SGFRIRPLSL EFWRDRPFRL HDRMFFDRPD LGSTWTVTRL YP 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000449 Genomic DNA. Translation: ABI65150.1.
RefSeqYP_756088.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0ARD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394221.Mmar10_0857.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI65150; ABI65150; Mmar10_0857.
GeneID4285858.
KEGGmmr:Mmar10_0857.
PATRIC22449742. VBIMarMar77530_0878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAAVLHWKS.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-867-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_MARMM
AccessionPrimary (citable) accession number: Q0ARD7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 58 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