Pyridoxine-5'-phosphate oxidase - Rattus norvegicus (Rat)

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O88794 (PNPO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyridoxine-5'-phosphate oxidase
EC=1.4.3.5

Alternative name(s):
Pyridoxamine-phosphate oxidase

Gene names

Name:

Pnpo

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Pyridoxine 5'-phosphate + O₂ = pyridoxal 5'-phosphate + H₂O₂.
Cofactor	Binds 1 FMN per subunit.
Pathway	Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit structure	Homodimer By similarity.
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.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Ligand	FMN Flavoprotein Pyridoxal phosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro pyridoxamine-phosphate oxidase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Pyridoxine-5'-phosphate oxidase

PRO_0000167785

Regions

Nucleotide binding

110 – 111

FMN By similarity

Nucleotide binding

174 – 175

FMN By similarity

Region

225 – 227

Substrate binding By similarity

Sites

Binding site

FMN By similarity

Binding site

FMN; via amide nitrogen By similarity

Binding site

100

Substrate By similarity

Binding site

117

FMN By similarity

Binding site

157

Substrate By similarity

Binding site

161

Substrate By similarity

Binding site

165

Substrate By similarity

Amino acid modifications

Modified residue

165

Phosphoserine By similarity

Modified residue

241

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O88794 [UniParc].

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

261

30,184

        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' referencesShow '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, 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.
IPI	IPI00212603.
RefSeq	NP_072123.1. NM_022601.2.
UniGene	Rn.158883.
3D structure databases
ProteinModelPortal	O88794.
SMR	O88794. Positions 49-261.
ModBase	Search...
Proteomic databases
PRIDE	O88794.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000073746; ENSRNOP00000067069; ENSRNOG00000046493.
GeneID	64533.
KEGG	rno:64533.
Organism-specific databases
CTD	55163.
RGD	621456. Pnpo.
Phylogenomic databases
GeneTree	ENSGT00390000011219.
HOVERGEN	HBG045634.
KO	K00275.
Enzyme and pathway databases
UniPathway	UPA00190; UER00304. UPA00190; UER00305.
Gene expression databases
Genevestigator	O88794.
Family and domain databases
Gene3D	2.30.110.10. 1 hit.
InterPro	IPR000659. Pyridox_Oxase. IPR019740. Pyridox_Oxase_CS. IPR011576. Pyridox_Oxase_FMN-bd. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN-bd. [Graphical view]
PANTHER	PTHR10851. PTHR10851. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
PIRSF	PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAM	SSF50475. FMN_binding. 1 hit.
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	613378.

Entry information

Entry name

PNPO_RAT

Accession

Primary (citable) accession number: O88794

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents