PNPO_RAT
ID PNPO_RAT Reviewed; 261 AA.
AC O88794;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pyridoxine-5'-phosphate oxidase;
DE EC=1.4.3.5 {ECO:0000269|PubMed:9601034};
DE AltName: Full=Pyridoxamine-phosphate oxidase;
GN Name=Pnpo;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9601034; DOI=10.1021/bi972983r;
RA Ngo E.O., LePage G.R., Thanassi J.W., Meisler N., Nutter L.M.;
RT "Absence of pyridoxine-5'-phosphate oxidase (PNPO) activity in neoplastic
RT cells: isolation, characterization, and expression of PNPO cDNA.";
RL Biochemistry 37:7741-7748(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 109-116; 164-181 AND 188-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC (PLP). {ECO:0000269|PubMed:9601034}.
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:0000305|PubMed:9601034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15818;
CC Evidence={ECO:0000305|PubMed:9601034};
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:0000269|PubMed:9601034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15150;
CC Evidence={ECO:0000305|PubMed:9601034};
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:0000305|PubMed:9601034}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC {ECO:0000305|PubMed:9601034}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NVS9}.
CC -!- TISSUE SPECIFICITY: Detected in adult liver.
CC {ECO:0000269|PubMed:9601034}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in fetal brain, and at high
CC levels in adult brain. {ECO:0000269|PubMed:9601034}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; U91561; AAC23707.1; -; mRNA.
DR EMBL; BC087016; AAH87016.1; -; mRNA.
DR RefSeq; NP_072123.1; NM_022601.2.
DR AlphaFoldDB; O88794; -.
DR SMR; O88794; -.
DR STRING; 10116.ENSRNOP00000067069; -.
DR iPTMnet; O88794; -.
DR PhosphoSitePlus; O88794; -.
DR SwissPalm; O88794; -.
DR jPOST; O88794; -.
DR PaxDb; O88794; -.
DR PRIDE; O88794; -.
DR Ensembl; ENSRNOT00000073746; ENSRNOP00000067069; ENSRNOG00000046493.
DR GeneID; 64533; -.
DR KEGG; rno:64533; -.
DR CTD; 55163; -.
DR RGD; 621456; Pnpo.
DR eggNOG; KOG2586; Eukaryota.
DR GeneTree; ENSGT00390000011219; -.
DR HOGENOM; CLU_032263_2_1_1; -.
DR InParanoid; O88794; -.
DR OMA; PEPNAMV; -.
DR OrthoDB; 1337072at2759; -.
DR PhylomeDB; O88794; -.
DR Reactome; R-RNO-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR PRO; PR:O88794; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000046493; Expressed in heart and 19 other tissues.
DR Genevisible; O88794; RN.
DR GO; GO:0010181; F:FMN binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:RGD.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:RGD.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase;
KW Phosphoprotein; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..261
FT /note="Pyridoxine-5'-phosphate oxidase"
FT /id="PRO_0000167785"
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:0007744|PubMed:22673903"
SQ SEQUENCE 261 AA; 30184 MW; C5684A180FE89B68 CRC64;
MTCGLLSVTV TFRRPAKWPG YFRHLCCRGA VMDLGPMRKS YRGDREAFEE AHLTSLDPMK
QFASWFEEAV QCPDIGEANA MCLATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE
LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD
REYLRKKNEE LGQLYREQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD
SPLGPMTHHG EEDWVYERLA P
