PNPO_HUMAN
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 03-AUG-2022, entry version 192.
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=0.10 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};
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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; 39.
DR IntAct; Q9NVS9; 13.
DR STRING; 9606.ENSP00000225573; -.
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 BioMuta; PNPO; -.
DR DMDM; 37082126; -.
DR REPRODUCTION-2DPAGE; IPI00018272; -.
DR EPD; Q9NVS9; -.
DR jPOST; Q9NVS9; -.
DR MassIVE; Q9NVS9; -.
DR MaxQB; Q9NVS9; -.
DR PaxDb; Q9NVS9; -.
DR PeptideAtlas; Q9NVS9; -.
DR PRIDE; Q9NVS9; -.
DR ProteomicsDB; 5700; -.
DR ProteomicsDB; 5726; -.
DR ProteomicsDB; 5748; -.
DR ProteomicsDB; 82855; -. [Q9NVS9-1]
DR Antibodypedia; 17803; 370 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 CTD; 55163; -.
DR DisGeNET; 55163; -.
DR GeneCards; 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 OMA; PEPNAMV; -.
DR PhylomeDB; Q9NVS9; -.
DR TreeFam; TF313411; -.
DR BioCyc; MetaCyc:HS03105-MON; -.
DR BRENDA; 1.4.3.5; 2681.
DR PathwayCommons; Q9NVS9; -.
DR Reactome; R-HSA-964975; Vitamins B6 activation to pyridoxal phosphate.
DR SABIO-RK; Q9NVS9; -.
DR SignaLink; Q9NVS9; -.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR BioGRID-ORCS; 55163; 28 hits in 1084 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 155 other tissues.
DR ExpressionAtlas; Q9NVS9; baseline and differential.
DR Genevisible; Q9NVS9; HS.
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:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR DisProt; DP00168; -.
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 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
