PNPO_BOVIN
ID PNPO_BOVIN Reviewed; 261 AA.
AC Q5E9K3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Pyridoxine-5'-phosphate oxidase;
DE EC=1.4.3.5 {ECO:0000250|UniProtKB:Q9NVS9};
DE AltName: Full=Pyridoxamine-phosphate oxidase;
GN Name=PNPO;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen reticulum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC (PLP). {ECO:0000250|UniProtKB:Q9NVS9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15818;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15150;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q9NVS9};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC {ECO:0000250|UniProtKB:Q9NVS9}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC {ECO:0000250|UniProtKB:Q9NVS9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NVS9}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; BT020917; AAX08934.1; -; mRNA.
DR EMBL; BC103208; AAI03209.1; -; mRNA.
DR RefSeq; NP_001014907.1; NM_001014907.1.
DR AlphaFoldDB; Q5E9K3; -.
DR SMR; Q5E9K3; -.
DR STRING; 9913.ENSBTAP00000016263; -.
DR PaxDb; Q5E9K3; -.
DR PRIDE; Q5E9K3; -.
DR Ensembl; ENSBTAT00000016263; ENSBTAP00000016263; ENSBTAG00000012259.
DR GeneID; 512573; -.
DR KEGG; bta:512573; -.
DR CTD; 55163; -.
DR VEuPathDB; HostDB:ENSBTAG00000012259; -.
DR VGNC; VGNC:33096; PNPO.
DR eggNOG; KOG2586; Eukaryota.
DR GeneTree; ENSGT00390000011219; -.
DR HOGENOM; CLU_032263_2_1_1; -.
DR InParanoid; Q5E9K3; -.
DR OMA; PEPNAMV; -.
DR OrthoDB; 1337072at2759; -.
DR TreeFam; TF313411; -.
DR Reactome; R-BTA-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000012259; Expressed in liver and 104 other tissues.
DR GO; GO:0010181; F:FMN binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; ISS:UniProtKB.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR HAMAP; MF_01629; PdxH; 1.
DR InterPro; IPR000659; Pyridox_Oxase.
DR InterPro; IPR019740; Pyridox_Oxase_CS.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR10851; PTHR10851; 1.
DR Pfam; PF10590; PNP_phzG_C; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR TIGRFAMs; TIGR00558; pdxH; 1.
DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; Oxidoreductase; Phosphoprotein; Pyridoxal phosphate;
KW Pyridoxine biosynthesis; Reference proteome.
FT CHAIN 1..261
FT /note="Pyridoxine-5'-phosphate oxidase"
FT /id="PRO_0000167782"
FT BINDING 42..45
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 95..98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 100
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 110..111
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 116..117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 157
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 161
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 165
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 174..175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 225..227
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 229
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
SQ SEQUENCE 261 AA; 30366 MW; 7BDBB5478C6704AD CRC64;
MIFWLRSVIV TFGRPAEWPR CLRHLCSRGA AMDLGPMRKT YRGDPEAFEE THLTSLDPVK
QFAAWFEEAV QCPDIMEANA MCLATCTRDG KPSARMVLLK GFGKDGFRFF TNFESRKGKE
LDSNPFASLV FYWEPLHRQV RVEGPVKKLP EEEAECYFHS RPKSSQIGAV VSHQSSVIPD
REYLRKKNKE LEQLYQEQEV PKPKYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLLTGD
SPLGPMTHRG EEDWVYERLA P
