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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
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 sitei74SubstrateUniRule annotation1
Binding sitei89FMNUniRule annotation1
Binding sitei90FMNUniRule annotation1
Binding sitei112FMNUniRule annotation1
Binding sitei130SubstrateUniRule annotation1
Binding sitei134SubstrateUniRule annotation1
Binding sitei138SubstrateUniRule annotation1
Binding sitei194FMNUniRule annotation1
Binding sitei204FMNUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi69 – 74FMNUniRule annotation6
Nucleotide bindingi83 – 84FMNUniRule annotation2
Nucleotide bindingi148 – 149FMNUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BioCyciACEL351607:G1G7K-122-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:Acel_0116
OrganismiAcidothermus cellulolyticus (strain ATCC 43068 / 11B)
Taxonomic identifieri351607 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaAcidothermalesAcidothermaceaeAcidothermus
Proteomesi
  • UP000008221 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002922811 – 224Pyridoxine/pyridoxamine 5'-phosphate oxidaseAdd BLAST224

Proteomic databases

PRIDEiA0LR32

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi351607.Acel_0116

Structurei

3D structure databases

ProteinModelPortaliA0LR32
SMRiA0LR32
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 202Substrate 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.

A0LR32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHGTHTGSN PYAEAYVEVT AGGLAETDLA ADPIEQFRRW LADAIRYNLP
60 70 80 90 100
EPTAMVVATA DADGRPSSRH VLLKSVDDGF VFFTNYRSRK GRDLSENPSA
110 120 130 140 150
SLCFPWFAIG RQVVVLGTVT KVTREETEEY FASRPRDSQC GAWSSENQSS
160 170 180 190 200
VVPSRAWLDE RYAEVAQRFA GVEHIPPPPF WGGFRVIPET VEFWQARPAR
210 220
MHDRLRYRRT ADGERPWIIE RLSP
Length:224
Mass (Da):25,428
Last modified:December 12, 2006 - v1
Checksum:iD50A98E36BA4A6B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000481 Genomic DNA Translation: ABK51892.1
RefSeqiWP_011718956.1, NC_008578.1

Genome annotation databases

EnsemblBacteriaiABK51892; ABK51892; Acel_0116
KEGGiace:Acel_0116

Similar proteinsi

Entry informationi

Entry nameiPDXH_ACIC1
AccessioniPrimary (citable) accession number: A0LR32
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 12, 2006
Last modified: May 23, 2018
This is version 69 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

Documents

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

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