Q5E9K3 (PNPO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.
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 By similarity.
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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: GOC 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 electronic annotation. Source: EC
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_0000167782
Regions
	Nucleotide binding	110 – 111	2	FMN By similarity
	Nucleotide binding	174 – 175	2	FMN By similarity
	Region	225 – 227	3	Substrate binding By similarity
Sites
	Binding site	95	1	FMN By similarity
	Binding site	98	1	FMN; via amide nitrogen By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	117	1	FMN By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
Amino acid modifications
	Modified residue	165	1	Phosphoserine By similarity
	Modified residue	241	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5E9K3 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 7BDBB5478C6704AD	FASTA	261	30,366
	10 20 30 40 50 60 MIFWLRSVIV TFGRPAEWPR CLRHLCSRGA AMDLGPMRKT YRGDPEAFEE THLTSLDPVK 70 80 90 100 110 120 QFAAWFEEAV QCPDIMEANA MCLATCTRDG KPSARMVLLK GFGKDGFRFF TNFESRKGKE 130 140 150 160 170 180 LDSNPFASLV FYWEPLHRQV RVEGPVKKLP EEEAECYFHS RPKSSQIGAV VSHQSSVIPD 190 200 210 220 230 240 REYLRKKNKE LEQLYQEQEV PKPKYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLLTGD 250 260 SPLGPMTHRG EEDWVYERLA P

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Rumen reticulum.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT020917 mRNA. Translation: AAX08934.1. BC103208 mRNA. Translation: AAI03209.1.
IPI	IPI00694129.
RefSeq	NP_001014907.1. NM_001014907.1.
UniGene	Bt.24214.
3D structure databases
ProteinModelPortal	Q5E9K3.
SMR	Q5E9K3. Positions 49-261.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000016263.
Proteomic databases
PRIDE	Q5E9K3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000016263; ENSBTAP00000016263; ENSBTAG00000012259.
GeneID	512573.
KEGG	bta:512573.
Organism-specific databases
CTD	55163.
Phylogenomic databases
eggNOG	COG0259.
GeneTree	ENSGT00390000011219.
HOGENOM	HOG000242755.
HOVERGEN	HBG045634.
InParanoid	Q5E9K3.
KO	K00275.
OMA	ERIEFWQ.
OrthoDB	EOG4CVG7G.
Enzyme and pathway databases
UniPathway	UPA00190; UER00304. UPA00190; UER00305.
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	20870451.

Entry information

Entry name

PNPO_BOVIN

Accession

Primary (citable) accession number: Q5E9K3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	March 15, 2005
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program