ID PNPO_HUMAN Reviewed; 261 AA. AC Q9NVS9; B4E0V0; B4E152; B4E1D7; D3DTT9; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Pyridoxine-5'-phosphate oxidase; DE EC=1.4.3.5 {ECO:0000269|PubMed:12824491, ECO:0000269|PubMed:15182361, ECO:0000269|PubMed:15772097}; DE AltName: Full=Pyridoxamine-phosphate oxidase; GN Name=PNPO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Kwon O.-S.; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Liver, Teratocarcinoma, Thymus, and Thyroid; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238 AND SER-241, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 49-161 IN COMPLEX WITH FMN AND RP PYRIDOXAL 5'-PHOSPHATE, PARTIAL PROTEIN SEQUENCE, SUBUNIT, ACTIVITY RP REGULATION, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=12824491; DOI=10.1110/ps.0356203; RA Musayev F.N., Di Salvo M.L., Ko T.-P., Schirch V., Safo M.K.; RT "Structure and properties of recombinant human pyridoxine 5'-phosphate RT oxidase."; RL Protein Sci. 12:1455-1463(2003). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF 1-MET--LEU-56; 1-MET--CYS-72 AND RP 238-TYR--PRO-261. RX PubMed=15182361; DOI=10.1111/j.1432-1033.2004.04175.x; RA Kang J.H., Hong M.L., Kim D.W., Park J., Kang T.C., Won M.H., Baek N.I., RA Moon B.J., Choi S.Y., Kwon O.S.; RT "Genomic organization, tissue distribution and deletion mutation of human RT pyridoxine 5'-phosphate oxidase."; RL Eur. J. Biochem. 271:2452-2461(2004). RN [11] RP VARIANT PNPOD TRP-229, VARIANT LYS-50, FUNCTION, CATALYTIC ACTIVITY, AND RP PATHWAY. RX PubMed=15772097; DOI=10.1093/hmg/ddi120; RA Mills P.B., Surtees R.A.H., Champion M.P., Beesley C.E., Dalton N., RA Scambler P.J., Heales S.J.R., Briddon A., Scheimberg I., Hoffmann G.F., RA Zschocke J., Clayton P.T.; RT "Neonatal epileptic encephalopathy caused by mutations in the PNPO gene RT encoding pyridox(am)ine 5'-phosphate oxidase."; RL Hum. Mol. Genet. 14:1077-1086(2005). RN [12] RP VARIANT PNPOD GLN-229. RX PubMed=23708187; DOI=10.1038/ng.2646; RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J., RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G., RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T., RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N., RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L., RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.; RT "Targeted resequencing in epileptic encephalopathies identifies de novo RT mutations in CHD2 and SYNGAP1."; RL Nat. Genet. 45:825-830(2013). RN [13] RP VARIANT PNPOD HIS-225. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). 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:12824491, ECO:0000269|PubMed:15182361, CC ECO:0000269|PubMed:15772097}. 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:12824491, ECO:0000269|PubMed:15182361}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15150; CC Evidence={ECO:0000305|PubMed:12824491, ECO:0000305|PubMed:15182361}; 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:0000269|PubMed:12824491, ECO:0000269|PubMed:15182361, CC ECO:0000269|PubMed:15772097}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15818; CC Evidence={ECO:0000305|PubMed:12824491, ECO:0000305|PubMed:15182361, CC ECO:0000305|PubMed:15772097}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:12824491}; CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:12824491}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.1 uM for pyridoxine 5'-phosphate {ECO:0000269|PubMed:15182361}; CC KM=6.2 uM for pyridoxamine 5'-phosphate CC {ECO:0000269|PubMed:15182361}; CC Vmax=0.1 umol/min/mg enzyme toward pyridoxine 5'-phosphate CC {ECO:0000269|PubMed:15182361}; CC Vmax=0.05 umol/min/mg enzyme toward pyridoxamine 5'-phosphate CC {ECO:0000269|PubMed:15182361}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000305|PubMed:12824491, ECO:0000305|PubMed:15772097}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC {ECO:0000305|PubMed:12824491}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12824491}. CC -!- INTERACTION: CC Q9NVS9; Q6RW13-2: AGTRAP; NbExp=6; IntAct=EBI-11030787, EBI-11522760; CC Q9NVS9; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-11030787, EBI-11522780; CC Q9NVS9; Q9H400: LIME1; NbExp=3; IntAct=EBI-11030787, EBI-2830566; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NVS9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NVS9-2; Sequence=VSP_058769, VSP_058770; CC Name=3; CC IsoId=Q9NVS9-3; Sequence=VSP_056410; CC Name=4; CC IsoId=Q9NVS9-4; Sequence=VSP_056411; CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in liver, brain, lung, CC prostate and stomach (at protein level). {ECO:0000269|PubMed:15182361}. CC -!- DISEASE: Pyridoxine-5'-phosphate oxidase deficiency (PNPOD) CC [MIM:610090]: The main feature of neonatal epileptic encephalopathy is CC the onset within hours of birth of a severe seizure disorder that does CC not respond to anticonvulsant drugs and can be fatal. Seizures can CC cease with the administration of PLP, being resistant to treatment with CC pyridoxine,. {ECO:0000269|PubMed:15772097, ECO:0000269|PubMed:23708187, CC ECO:0000269|PubMed:27864847}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG64562.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF468030; AAM76918.1; -; mRNA. DR EMBL; AK001397; BAA91668.1; -; mRNA. DR EMBL; AK303536; BAG64562.1; ALT_SEQ; mRNA. DR EMBL; AK303665; BAG64664.1; -; mRNA. DR EMBL; AK303792; BAG64749.1; -; mRNA. DR EMBL; CH471109; EAW94770.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94771.1; -; Genomic_DNA. DR EMBL; BC006525; AAH06525.1; -; mRNA. DR CCDS; CCDS11522.1; -. [Q9NVS9-1] DR RefSeq; NP_060599.1; NM_018129.3. [Q9NVS9-1] DR RefSeq; XP_011523270.1; XM_011524968.2. DR PDB; 1NRG; X-ray; 1.95 A; A=1-261. DR PDB; 3HY8; X-ray; 2.50 A; A=1-261. DR PDB; 6H00; X-ray; 1.66 A; A=1-261. DR PDBsum; 1NRG; -. DR PDBsum; 3HY8; -. DR PDBsum; 6H00; -. DR AlphaFoldDB; Q9NVS9; -. DR SMR; Q9NVS9; -. DR BioGRID; 120463; 43. DR IntAct; Q9NVS9; 14. DR STRING; 9606.ENSP00000493302; -. DR BindingDB; Q9NVS9; -. DR ChEMBL; CHEMBL3271932; -. DR DrugBank; DB03247; Flavin mononucleotide. DR DrugBank; DB03345; Mercaptoethanol. DR DrugBank; DB00114; Pyridoxal phosphate. DR DrugBank; DB02209; Pyridoxine phosphate. DR DrugCentral; Q9NVS9; -. DR GlyGen; Q9NVS9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NVS9; -. DR MetOSite; Q9NVS9; -. DR PhosphoSitePlus; Q9NVS9; -. DR SwissPalm; Q9NVS9; -. DR BioMuta; PNPO; -. DR DMDM; 37082126; -. DR REPRODUCTION-2DPAGE; IPI00018272; -. DR EPD; Q9NVS9; -. DR jPOST; Q9NVS9; -. DR MassIVE; Q9NVS9; -. DR MaxQB; Q9NVS9; -. DR PaxDb; 9606-ENSP00000225573; -. DR PeptideAtlas; Q9NVS9; -. DR ProteomicsDB; 5700; -. DR ProteomicsDB; 5726; -. DR ProteomicsDB; 5748; -. DR ProteomicsDB; 82855; -. [Q9NVS9-1] DR Pumba; Q9NVS9; -. DR Antibodypedia; 17803; 409 antibodies from 26 providers. DR DNASU; 55163; -. DR Ensembl; ENST00000225573.5; ENSP00000225573.5; ENSG00000108439.11. [Q9NVS9-4] DR Ensembl; ENST00000434554.7; ENSP00000399960.3; ENSG00000108439.11. [Q9NVS9-3] DR Ensembl; ENST00000582171.6; ENSP00000463994.1; ENSG00000108439.11. [Q9NVS9-2] DR Ensembl; ENST00000585320.5; ENSP00000462345.1; ENSG00000108439.11. [Q9NVS9-2] DR Ensembl; ENST00000641856.1; ENSP00000493224.1; ENSG00000108439.11. [Q9NVS9-2] DR Ensembl; ENST00000642017.2; ENSP00000493302.2; ENSG00000108439.11. [Q9NVS9-1] DR GeneID; 55163; -. DR KEGG; hsa:55163; -. DR MANE-Select; ENST00000642017.2; ENSP00000493302.2; NM_018129.4; NP_060599.1. DR UCSC; uc010wlb.3; human. [Q9NVS9-1] DR AGR; HGNC:30260; -. DR CTD; 55163; -. DR DisGeNET; 55163; -. DR GeneCards; PNPO; -. DR GeneReviews; PNPO; -. DR HGNC; HGNC:30260; PNPO. DR HPA; ENSG00000108439; Tissue enhanced (liver). DR MalaCards; PNPO; -. DR MIM; 603287; gene. DR MIM; 610090; phenotype. DR neXtProt; NX_Q9NVS9; -. DR OpenTargets; ENSG00000108439; -. DR Orphanet; 79096; Pyridoxal phosphate-responsive seizures. DR PharmGKB; PA134915565; -. DR VEuPathDB; HostDB:ENSG00000108439; -. DR eggNOG; KOG2586; Eukaryota. DR GeneTree; ENSGT00390000011219; -. DR HOGENOM; CLU_032263_2_1_1; -. DR InParanoid; Q9NVS9; -. DR OMA; AYFRTRP; -. DR OrthoDB; 2873954at2759; -. DR PhylomeDB; Q9NVS9; -. DR TreeFam; TF313411; -. DR BioCyc; MetaCyc:HS03105-MONOMER; -. DR BRENDA; 1.4.3.5; 2681. DR PathwayCommons; Q9NVS9; -. DR Reactome; R-HSA-964975; Vitamin B6 activation to pyridoxal phosphate. DR SABIO-RK; Q9NVS9; -. DR SignaLink; Q9NVS9; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR BioGRID-ORCS; 55163; 31 hits in 1165 CRISPR screens. DR ChiTaRS; PNPO; human. DR EvolutionaryTrace; Q9NVS9; -. DR GeneWiki; PNPO; -. DR GenomeRNAi; 55163; -. DR Pharos; Q9NVS9; Tchem. DR PRO; PR:Q9NVS9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9NVS9; Protein. DR Bgee; ENSG00000108439; Expressed in right lobe of liver and 157 other cell types or tissues. DR ExpressionAtlas; Q9NVS9; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0010181; F:FMN binding; IDA:CAFA. DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:CAFA. DR GO; GO:0004733; F:pyridoxamine phosphate oxidase activity; IDA:UniProtKB. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:CAFA. DR GO; GO:0042818; P:pyridoxamine metabolic process; IEA:Ensembl. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR DisProt; DP00168; -. 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 NCBIfam; TIGR00558; pdxH; 1. DR PANTHER; PTHR10851:SF0; PYRIDOXINE-5'-PHOSPHATE OXIDASE; 1. DR PANTHER; PTHR10851; PYRIDOXINE-5-PHOSPHATE OXIDASE; 1. DR Pfam; PF10590; PNP_phzG_C; 1. DR Pfam; PF01243; Putative_PNPOx; 1. DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1. DR SUPFAM; SSF50475; FMN-binding split barrel; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. DR Genevisible; Q9NVS9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease variant; Epilepsy; 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_0000167783" 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:0000269|PubMed:12824491" FT BINDING 100 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:12824491" FT BINDING 110..111 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:12824491" FT BINDING 116..117 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:12824491" 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:0000269|PubMed:12824491" FT BINDING 161 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:12824491" FT BINDING 165 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:12824491" FT BINDING 174..175 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:12824491" 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:0007744|PubMed:24275569" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 47..69 FT /note="AFEETHLTSLDPVKQFAAWFEEA -> RWKTLCSHVAAEGLRERWLPLLH FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_058769" FT VAR_SEQ 70..261 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_058770" FT VAR_SEQ 122..139 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056410" FT VAR_SEQ 140..182 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056411" FT VARIANT 50 FT /note="E -> K (in dbSNP:rs549477447)" FT /evidence="ECO:0000269|PubMed:15772097" FT /id="VAR_029358" FT VARIANT 116 FT /note="R -> Q (in dbSNP:rs17679445)" FT /id="VAR_029359" FT VARIANT 225 FT /note="R -> H (in PNPOD; dbSNP:rs550423482)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078229" FT VARIANT 229 FT /note="R -> Q (in PNPOD; dbSNP:rs773450573)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078643" FT VARIANT 229 FT /note="R -> W (in PNPOD; strong activity decrease; FT dbSNP:rs104894629)" FT /evidence="ECO:0000269|PubMed:15772097" FT /id="VAR_029360" FT MUTAGEN 1..72 FT /note="Missing: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:15182361" FT MUTAGEN 1..56 FT /note="Missing: Has no effect on the catalytic activity." FT /evidence="ECO:0000269|PubMed:15182361" FT MUTAGEN 238..261 FT /note="Missing: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:15182361" FT HELIX 58..71 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:3HY8" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:3HY8" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:6H00" FT HELIX 116..123 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 126..133 FT /evidence="ECO:0007829|PDB:6H00" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 138..148 FT /evidence="ECO:0007829|PDB:6H00" FT HELIX 151..159 FT /evidence="ECO:0007829|PDB:6H00" FT HELIX 163..171 FT /evidence="ECO:0007829|PDB:6H00" FT HELIX 181..194 FT /evidence="ECO:0007829|PDB:6H00" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:6H00" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:6H00" SQ SEQUENCE 261 AA; 29988 MW; 2C74E9F962FE2A95 CRC64; MTCWLRGVTA TFGRPAEWPG YLSHLCGRSA AMDLGPMRKS YRGDREAFEE THLTSLDPVK QFAAWFEEAV QCPDIGEANA MCLATCTRDG KPSARMLLLK GFGKDGFRFF TNFESRKGKE LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EEEAECYFHS RPKSSQIGAV VSHQSSVIPD REYLRKKNEE LEQLYQDQEV PKPKSWGGYV LYPQVMEFWQ GQTNRLHDRI VFRRGLPTGD SPLGPMTHRG EEDWLYERLA P //