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O88794 (PNPO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxine-5'-phosphate oxidase

EC=1.4.3.5
Alternative name(s):
Pyridoxamine-phosphate oxidase
Gene names
Name:Pnpo
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule MF_01629

Cofactor

Binds 1 FMN per subunit.

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP-Rule MF_01629

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01629

Tissue specificity

Detected in adult liver. Ref.1

Developmental stage

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

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Pyridoxine-5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167785

Regions

Nucleotide binding110 – 1112FMN By similarity
Nucleotide binding174 – 1752FMN By similarity
Region225 – 2273Substrate binding By similarity

Sites

Binding site951FMN By similarity
Binding site981FMN; via amide nitrogen By similarity
Binding site1001Substrate By similarity
Binding site1171FMN By similarity
Binding site1571Substrate By similarity
Binding site1611Substrate By similarity
Binding site1651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O88794 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C5684A180FE89B68

FASTA26130,184
        10         20         30         40         50         60 
MTCGLLSVTV TFRRPAKWPG YFRHLCCRGA VMDLGPMRKS YRGDREAFEE AHLTSLDPMK 

        70         80         90        100        110        120 
QFASWFEEAV QCPDIGEANA MCLATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE 

       130        140        150        160        170        180 
LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD 

       190        200        210        220        230        240 
REYLRKKNEE LGQLYREQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD 

       250        260 
SPLGPMTHHG EEDWVYERLA P 

« Hide

References

« Hide 'large scale' references
[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(1998) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U91561 mRNA. Translation: AAC23707.1.
BC087016 mRNA. Translation: AAH87016.1.
RefSeqNP_072123.1. NM_022601.2.
UniGeneRn.158883.

3D structure databases

ProteinModelPortalO88794.
SMRO88794. Positions 49-261.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO88794.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000073746; ENSRNOP00000067069; ENSRNOG00000046493.
GeneID64533.
KEGGrno:64533.

Organism-specific databases

CTD55163.
RGD621456. Pnpo.

Phylogenomic databases

GeneTreeENSGT00390000011219.
HOVERGENHBG045634.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG7B8S4P.
PhylomeDBO88794.

Enzyme and pathway databases

UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Gene expression databases

GenevestigatorO88794.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613378.
PROO88794.

Entry information

Entry namePNPO_RAT
AccessionPrimary (citable) accession number: O88794
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways