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A3PIG5 (PDXH_RHOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Rsph17029_1020
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length200 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 – 200200Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292320

Regions

Nucleotide binding63 – 642FMN By similarity
Nucleotide binding127 – 1282FMN By similarity
Region177 – 1793Substrate binding By similarity

Sites

Binding site481FMN By similarity
Binding site511FMN; via amide nitrogen By similarity
Binding site531Substrate By similarity
Binding site701FMN By similarity
Binding site1101Substrate By similarity
Binding site1141Substrate By similarity
Binding site1181Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PIG5 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 976FA9210D5128A1

FASTA20022,477
        10         20         30         40         50         60 
MDRTGIFAGD DPFAIAAGWL AEAEPQEPND PNAIALATVD AAGLPNVRMV LLKEIEAEAF 

        70         80         90        100        110        120 
VFYTNYGSQK AVEIETSGKA AFVLHWKSLR RQIRVRGLVE REEGVQADAY YASRSLKSRL 

       130        140        150        160        170        180 
GAWASEQSRP LASRTSLLAE VARVTARFGT NPPRPAFWGG FRIRPLEIEF WADGAFRLHD 

       190        200 
RFRWRRNSLS DGWSIERLNP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."
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., Kiss H., 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., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000577 Genomic DNA. Translation: ABN76131.1.
RefSeqYP_001042903.1. NC_009049.1.

3D structure databases

ProteinModelPortalA3PIG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349101.Rsph17029_1020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN76131; ABN76131; Rsph17029_1020.
GeneID4897518.
KEGGrsh:Rsph17029_1020.
PATRIC23169758. VBIRhoSph114483_1191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMASIEFWCD.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycRSPH349101:GHC8-1039-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_RHOS1
AccessionPrimary (citable) accession number: A3PIG5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 51 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