PNPO_MOUSE
ID PNPO_MOUSE Reviewed; 261 AA.
AC Q91XF0; Q3TP70; Q3U445; Q3U4X1;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Stomach, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Liver;
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 [4]
RP PROTEIN SEQUENCE OF 120-138, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK154004; BAE32309.1; -; mRNA.
DR EMBL; AK154443; BAE32590.1; ALT_INIT; mRNA.
DR EMBL; AK164667; BAE37867.1; -; mRNA.
DR EMBL; AL596384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010785; AAH10785.1; -; mRNA.
DR EMBL; BC026564; AAH26564.1; -; mRNA.
DR CCDS; CCDS25308.1; -.
DR RefSeq; NP_598782.1; NM_134021.2.
DR AlphaFoldDB; Q91XF0; -.
DR SMR; Q91XF0; -.
DR STRING; 10090.ENSMUSP00000018803; -.
DR ChEMBL; CHEMBL3271931; -.
DR iPTMnet; Q91XF0; -.
DR PhosphoSitePlus; Q91XF0; -.
DR EPD; Q91XF0; -.
DR jPOST; Q91XF0; -.
DR MaxQB; Q91XF0; -.
DR PaxDb; Q91XF0; -.
DR PeptideAtlas; Q91XF0; -.
DR PRIDE; Q91XF0; -.
DR ProteomicsDB; 289712; -.
DR Antibodypedia; 17803; 370 antibodies from 26 providers.
DR DNASU; 103711; -.
DR Ensembl; ENSMUST00000018803; ENSMUSP00000018803; ENSMUSG00000018659.
DR GeneID; 103711; -.
DR KEGG; mmu:103711; -.
DR UCSC; uc007ldc.1; mouse.
DR CTD; 55163; -.
DR MGI; MGI:2144151; Pnpo.
DR VEuPathDB; HostDB:ENSMUSG00000018659; -.
DR eggNOG; KOG2586; Eukaryota.
DR GeneTree; ENSGT00390000011219; -.
DR HOGENOM; CLU_032263_2_1_1; -.
DR InParanoid; Q91XF0; -.
DR OMA; PEPNAMV; -.
DR OrthoDB; 1337072at2759; -.
DR PhylomeDB; Q91XF0; -.
DR TreeFam; TF313411; -.
DR Reactome; R-MMU-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR BioGRID-ORCS; 103711; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pnpo; mouse.
DR PRO; PR:Q91XF0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91XF0; protein.
DR Bgee; ENSMUSG00000018659; Expressed in fetal liver hematopoietic progenitor cell and 262 other tissues.
DR ExpressionAtlas; Q91XF0; baseline and differential.
DR Genevisible; Q91XF0; MM.
DR GO; GO:0010181; F:FMN binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; ISS:UniProtKB.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; ISO:MGI.
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_0000167784"
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:21183079"
SQ SEQUENCE 261 AA; 30114 MW; D83A54883B4BC0EC CRC64;
MTCGLLSVTV TFRRPAKWTG YLRHLCCRGA VMDLGPMRKS YRGDREAFEE THLTSLDPMK
QFASWFDEAV QCPDIGEANA MCVATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE
LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD
REYLRKKNEE LGQLYQDQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD
SPLGPMTHHG EEDWVYERLA P
