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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Blochmannia pennsylvanicus (strain BPEN)
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 (pdxH)
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 (pdxH)
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 sitei70SubstrateUniRule annotation1
Binding sitei86FMNUniRule annotation1
Binding sitei87FMNUniRule annotation1
Binding sitei109FMNUniRule annotation1
Binding sitei127SubstrateUniRule annotation1
Binding sitei131SubstrateUniRule annotation1
Binding sitei189FMNUniRule annotation1
Binding sitei199FMNUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi65 – 70FMNUniRule annotation6
Nucleotide bindingi80 – 81FMNUniRule annotation2
Nucleotide bindingi144 – 145FMNUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BioCyciCBLO291272:G1G3Y-376-MONOMER
UniPathwayiUPA01068; UER00304
UPA01068; UER00305

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidaseUniRule annotation (EC:1.4.3.5UniRule annotation)
Alternative name(s):
PNP/PMP oxidaseUniRule annotation
Short name:
PNPOxUniRule annotation
Pyridoxal 5'-phosphate synthaseUniRule annotation
Gene namesi
Name:pdxHUniRule annotation
Ordered Locus Names:BPEN_381
OrganismiBlochmannia pennsylvanicus (strain BPEN)
Taxonomic identifieri291272 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia
Proteomesi
  • UP000007794 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676881 – 216Pyridoxine/pyridoxamine 5'-phosphate oxidaseAdd BLAST216

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi291272.BPEN_381

Structurei

3D structure databases

ProteinModelPortaliQ492T8
SMRiQ492T8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni12 – 15Substrate bindingUniRule annotation4
Regioni195 – 197Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108S7T Bacteria
COG0259 LUCA
HOGENOMiHOG000242755
KOiK00275
OMAiPEPNAMV
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.

Q492T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIDKTNISN IRREYISGQL RHTDLTNQPI QLFSVWLHQA YFSKIPDPTA
60 70 80 90 100
MCLATVDHTG QPYQRVVLLK NFTNKEMIFY TNLSSRKAMH LANNPKVSLC
110 120 130 140 150
FLWNVIDRQV IITGSVDKLP EKEVLKYFYT RPKNNQISTW VSNQSKVISS
160 170 180 190 200
KDLLENKFLE FKKNHLHKKV PFPEFWGGYK ININSMEFWQ GGTHRLHDRF
210
IYQRYKHTWR IYRLSP
Length:216
Mass (Da):25,738
Last modified:September 13, 2005 - v1
Checksum:iCC87E55758F56C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000016 Genomic DNA Translation: AAZ41005.1
RefSeqiWP_011282914.1, NC_007292.1

Genome annotation databases

EnsemblBacteriaiAAZ41005; AAZ41005; BPEN_381
KEGGibpn:BPEN_381

Similar proteinsi

Entry informationi

Entry nameiPDXH_BLOPB
AccessioniPrimary (citable) accession number: Q492T8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: April 25, 2018
This is version 89 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, Reference proteome
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Main funding by: National Institutes of Health