ID   PNPO_DICDI              Reviewed;         227 AA.
AC   Q54YS6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
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; ORFNames=DDB_G0278107;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000023; EAL68226.1; -; Genomic_DNA.
DR   RefSeq; XP_642126.1; XM_637034.1.
DR   AlphaFoldDB; Q54YS6; -.
DR   SMR; Q54YS6; -.
DR   STRING; 44689.Q54YS6; -.
DR   PaxDb; 44689-DDB0231657; -.
DR   EnsemblProtists; EAL68226; EAL68226; DDB_G0278107.
DR   GeneID; 8621335; -.
DR   KEGG; ddi:DDB_G0278107; -.
DR   dictyBase; DDB_G0278107; -.
DR   eggNOG; KOG2586; Eukaryota.
DR   HOGENOM; CLU_032263_2_3_1; -.
DR   InParanoid; Q54YS6; -.
DR   OMA; AYFRTRP; -.
DR   PhylomeDB; Q54YS6; -.
DR   Reactome; R-DDI-964975; Vitamin B6 activation to pyridoxal phosphate.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   PRO; PR:Q54YS6; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004733; F:pyridoxamine phosphate oxidase activity; ISS:dictyBase.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase; Phosphoprotein; Pyridoxal phosphate;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN           1..227
FT                   /note="Pyridoxine-5'-phosphate oxidase"
FT                   /id="PRO_0000331120"
FT   BINDING         20..23
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         75..78
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         90..91
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         96..97
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         117
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         135
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         139
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         143
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         152..153
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         197
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         203..205
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         207
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
SQ   SEQUENCE   227 AA;  26850 MW;  3EBA15FAEED2A3FE CRC64;
     MSINLDNEEL KNEDLVANMR KDYRMGELKE EGLLESPFKM FDMWLTQEIE LKNEGAEPNA
     FTLATCSIER KPSARVVLLK HFDHQGFVFY TNYNSRKSKE LSENPFASMT FLWTQKQVRI
     EGSVEKVDRL ESEKYFKSRP RSSQIGAWVS EFQSSEVTKQ HLEEKTIEME NKFKDQEVPL
     PPFWGGWRIK PYAFEFWQGK SGRIHDRFKY VPTDSNNDNW ITKRLSP
//