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Protein

Pyridoxine-5'-phosphate oxidase

Gene

Pnpo

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).1 Publication

Catalytic activityi

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

Cofactori

FMNNote: Binds 1 FMN per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951FMNBy similarity
Binding sitei98 – 981FMN; via amide nitrogenBy similarity
Binding sitei100 – 1001SubstrateBy similarity
Binding sitei117 – 1171FMNBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei161 – 1611SubstrateBy similarity
Binding sitei165 – 1651SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1112FMNBy similarity
Nucleotide bindingi174 – 1752FMNBy similarity

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. pyridoxamine-phosphate oxidase activity Source: RGD

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: GOC
  2. pyridoxine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_278426. Vitamins B6 activation to pyridoxal phosphate.
UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine-5'-phosphate oxidase (EC:1.4.3.5)
Alternative name(s):
Pyridoxamine-phosphate oxidase
Gene namesi
Name:Pnpo
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi621456. Pnpo.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Pyridoxine-5'-phosphate oxidasePRO_0000167785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381PhosphothreonineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO88794.

Expressioni

Tissue specificityi

Detected in adult liver.1 Publication

Developmental stagei

Detected at low levels in fetal brain, and at high levels in adult brain.1 Publication

Gene expression databases

GenevestigatoriO88794.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

SMRiO88794. Positions 49-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 2273Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000011219.
HOVERGENiHBG045634.
InParanoidiO88794.
KOiK00275.
OMAiPHWGGFR.
OrthoDBiEOG7B8S4P.
PhylomeDBiO88794.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851. PTHR10851. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTCGLLSVTV TFRRPAKWPG YFRHLCCRGA VMDLGPMRKS YRGDREAFEE
60 70 80 90 100
AHLTSLDPMK QFASWFEEAV QCPDIGEANA MCLATCTRDG KPSARMLLLK
110 120 130 140 150
GFGKDGFRFF TNYESRKGKE LDSNPFASLV FYWEPLNRQV RVEGPVKKLP
160 170 180 190 200
EKEAENYFHS RPKSSQIGAV VSRQSSVIPD REYLRKKNEE LGQLYREQEV
210 220 230 240 250
PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD SPLGPMTHHG
260
EEDWVYERLA P
Length:261
Mass (Da):30,184
Last modified:October 31, 1998 - v1
Checksum:iC5684A180FE89B68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91561 mRNA. Translation: AAC23707.1.
BC087016 mRNA. Translation: AAH87016.1.
RefSeqiNP_072123.1. NM_022601.2.
UniGeneiRn.158883.

Genome annotation databases

EnsembliENSRNOT00000073746; ENSRNOP00000067069; ENSRNOG00000046493.
GeneIDi64533.
KEGGirno:64533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91561 mRNA. Translation: AAC23707.1.
BC087016 mRNA. Translation: AAH87016.1.
RefSeqiNP_072123.1. NM_022601.2.
UniGeneiRn.158883.

3D structure databases

SMRiO88794. Positions 49-261.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO88794.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000073746; ENSRNOP00000067069; ENSRNOG00000046493.
GeneIDi64533.
KEGGirno:64533.

Organism-specific databases

CTDi55163.
RGDi621456. Pnpo.

Phylogenomic databases

GeneTreeiENSGT00390000011219.
HOVERGENiHBG045634.
InParanoidiO88794.
KOiK00275.
OMAiPHWGGFR.
OrthoDBiEOG7B8S4P.
PhylomeDBiO88794.

Enzyme and pathway databases

UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.
ReactomeiREACT_278426. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

NextBioi613378.
PROiO88794.

Gene expression databases

GenevestigatoriO88794.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851. PTHR10851. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Absence of pyridoxine-5'-phosphate oxidase (PNPO) activity in neoplastic cells: isolation, characterization, and expression of PNPO cDNA."
    Ngo E.O., LePage G.R., Thanassi J.W., Meisler N., Nutter L.M.
    Biochemistry 37:7741-7748(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 109-116; 164-181 AND 188-196, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiPNPO_RAT
AccessioniPrimary (citable) accession number: O88794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 25, 2003
Last sequence update: October 31, 1998
Last modified: March 31, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.