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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Albidiferax ferrireducens)
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 sitei66SubstrateUniRule annotation1
Binding sitei82FMNUniRule annotation1
Binding sitei83FMNUniRule annotation1
Binding sitei123SubstrateUniRule annotation1
Binding sitei127SubstrateUniRule annotation1
Binding sitei131SubstrateUniRule annotation1
Binding sitei184FMNUniRule annotation1
Binding sitei194FMNUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 66FMNUniRule annotation6
Nucleotide bindingi76 – 77FMNUniRule annotation2
Nucleotide bindingi140 – 141FMNUniRule 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 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:Rfer_2059
OrganismiRhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Albidiferax ferrireducens)
Taxonomic identifieri338969 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002558831 – 220Pyridoxine/pyridoxamine 5'-phosphate oxidaseAdd BLAST220

Proteomic databases

PRIDEiQ21WR9

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi338969.Rfer_2059

Structurei

3D structure databases

ProteinModelPortaliQ21WR9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 11Substrate bindingUniRule annotation4
Regioni190 – 192Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108S7T Bacteria
COG0259 LUCA
HOGENOMiHOG000242755
KOiK00275
OrthoDBiPOG091H054N

Family and domain databases

Gene3Di2.30.110.10, 1 hit
HAMAPiMF_01629 PdxH, 1 hit
InterProiView protein in InterPro
IPR000659 Pyridox_Oxase
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

Sequencei

Sequence statusi: Complete.

Q21WR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSIAHLRKS YERAELSEDA SHADPLQQFE KWLKEAISAE IPEPNAMTVA
60 70 80 90 100
TVASNLRPST RVVLIKGYDE RGITWFTNYD SRKGQELAGN PYAALQFHWV
110 120 130 140 150
ELERVVRIEG IVEKVSEEES DSYFHSRPLD SRIGAWASPQ SQVISGRSVL
160 170 180 190 200
VANAAKYGAK FLLNPPRPPH WGGYRLKPDH WQFWQGRKSR LHDRLRYTLI
210 220
EPASTLPDAK PVWIRERLAP
Length:220
Mass (Da):25,187
Last modified:October 31, 2006 - v2
Checksum:iB452165F3E3B73BC
GO

Sequence cautioni

The sequence ABD69784 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000267 Genomic DNA Translation: ABD69784.1 Different initiation.
RefSeqiWP_041790548.1, NC_007908.1

Genome annotation databases

EnsemblBacteriaiABD69784; ABD69784; Rfer_2059
KEGGirfr:Rfer_2059

Entry informationi

Entry nameiPDXH_RHOFT
AccessioniPrimary (citable) accession number: Q21WR9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 23, 2018
This is version 78 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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