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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase 2

Gene

pdxH2

Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).UniRule annotation

Catalytic activityi

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.UniRule annotation
Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.UniRule annotation

Cofactori

FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Pyridoxine/pyridoxamine 5'-phosphate oxidase 2 (pdxH2), Pyridoxine/pyridoxamine 5'-phosphate oxidase 1 (pdxH1)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Pyridoxine/pyridoxamine 5'-phosphate oxidase 2 (pdxH2), Pyridoxine/pyridoxamine 5'-phosphate oxidase 1 (pdxH1)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65SubstrateUniRule annotation1
Binding sitei82FMNUniRule annotation1
Binding sitei104FMNUniRule annotation1
Binding sitei122SubstrateUniRule annotation1
Binding sitei126SubstrateUniRule annotation1
Binding sitei130SubstrateUniRule annotation1
Binding sitei184FMNUniRule annotation1
Binding sitei194FMNUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi60 – 65FMNUniRule annotation6
Nucleotide bindingi75 – 76FMNUniRule annotation2
Nucleotide bindingi139 – 140FMNUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

UniPathwayiUPA01068; UER00304
UPA01068; UER00305

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidase 2UniRule annotation (EC:1.4.3.5UniRule annotation)
Alternative name(s):
PNP/PMP oxidase 2UniRule annotation
Short name:
PNPOx 2UniRule annotation
Pyridoxal 5'-phosphate synthase 2UniRule annotation
Gene namesi
Name:pdxH2UniRule annotation
Ordered Locus Names:RSp0678
ORF Names:RS01771
Encoded oniPlasmid megaplasmid Rsp0 Publication
OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Taxonomic identifieri267608 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
Proteomesi
  • UP000001436 Componenti: Plasmid megaplasmid Rsp

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001677451 – 213Pyridoxine/pyridoxamine 5'-phosphate oxidase 2Add BLAST213

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8XS03
SMRiQ8XS03
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 192Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the pyridoxamine 5'-phosphate oxidase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242755
KOiK00275
OMAiRGWHFAT
OrthoDBiPOG091H054N

Family and domain databases

Gene3Di2.30.110.10, 1 hit
HAMAPiMF_01629 PdxH, 1 hit
InterProiView protein in InterPro
IPR000659 Pyridox_Oxase
IPR019740 Pyridox_Oxase_CS
IPR011576 Pyridox_Oxase_put
IPR019576 Pyridoxamine_oxidase_dimer_C
IPR012349 Split_barrel_FMN-bd
PANTHERiPTHR10851:SF0 PTHR10851:SF0, 1 hit
PfamiView protein in Pfam
PF10590 PNP_phzG_C, 1 hit
PF01243 Putative_PNPOx, 1 hit
PIRSFiPIRSF000190 Pyd_amn-ph_oxd, 1 hit
TIGRFAMsiTIGR00558 pdxH, 1 hit
PROSITEiView protein in PROSITE
PS01064 PYRIDOX_OXIDASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q8XS03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNATDMDTEA AFRNDHETIA GEDPFAMFGE WLELAHRKEI NDANAMALAT
60 70 80 90 100
ADPDGLPNVR MVLLKGFDRE GFVFYTNTES QKGVELAENM QAAAVLHWKS
110 120 130 140 150
LRRQVRFRGT VNRVSAEEAD AYFVSRARAS RIGAWASKQS RPLENRTALA
160 170 180 190 200
KSVATEAARF GISDIPRPAF WTGFRIVPNC IEFWMDKPFR LHDRLVFKRS
210
HSGEPWSALK LYP
Length:213
Mass (Da):24,165
Last modified:March 1, 2002 - v1
Checksum:iF6DE5C28CAB72266
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL646053 Genomic DNA Translation: CAD17829.1

Genome annotation databases

EnsemblBacteriaiCAD17829; CAD17829; RSp0678
KEGGirso:RSp0678

Similar proteinsi

Entry informationi

Entry nameiPDXH2_RALSO
AccessioniPrimary (citable) accession number: Q8XS03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2002
Last modified: March 28, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Plasmid, Reference proteome
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Main funding by: National Institutes of Health