PDXH_CAEEL
ID PDXH_CAEEL Reviewed; 226 AA.
AC Q20939;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Putative pyridoxamine 5'-phosphate oxidase;
DE EC=1.4.3.5;
DE AltName: Full=PNP/PMP oxidase;
DE Short=PNPOx;
GN ORFNames=F57B9.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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}.
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 -!- 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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; FO081266; CCD70322.1; -; Genomic_DNA.
DR PIR; A88494; A88494.
DR RefSeq; NP_498518.2; NM_066117.3.
DR AlphaFoldDB; Q20939; -.
DR SMR; Q20939; -.
DR BioGRID; 41187; 1.
DR IntAct; Q20939; 1.
DR STRING; 6239.F57B9.1; -.
DR EPD; Q20939; -.
DR PaxDb; Q20939; -.
DR PeptideAtlas; Q20939; -.
DR EnsemblMetazoa; F57B9.1.1; F57B9.1.1; WBGene00018996.
DR EnsemblMetazoa; F57B9.1.2; F57B9.1.2; WBGene00018996.
DR GeneID; 175973; -.
DR UCSC; F57B9.1; c. elegans.
DR CTD; 175973; -.
DR WormBase; F57B9.1; CE44186; WBGene00018996; -.
DR eggNOG; KOG2586; Eukaryota.
DR GeneTree; ENSGT00390000011219; -.
DR HOGENOM; CLU_032263_2_1_1; -.
DR InParanoid; Q20939; -.
DR OMA; EINDANA; -.
DR OrthoDB; 1337072at2759; -.
DR PhylomeDB; Q20939; -.
DR Reactome; R-CEL-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR PRO; PR:Q20939; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018996; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Putative pyridoxamine 5'-phosphate oxidase"
FT /id="PRO_0000167788"
FT BINDING 16..19
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 72..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 87..88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 93..94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 134
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 138
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 142
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 151..152
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 205..207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 209
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
SQ SEQUENCE 226 AA; 26101 MW; 99E80C34C740AE2B CRC64;
METPSIDIQN IRAKYLNSHD PYLLESKLPT TSPFELFDIW FRNVASQSDL TFEEINAVSL
STVGKDLRPS SRMVLLKAYT PTGFSFYTNY TSRKGNQLEE NPNAAMLFYW PKVNRQIRVE
GVVEKLPDEM AVAYWNSRPV ASRIGSKSSD QSKVVPDREF LESKKVALTE LSVREGAQAI
TKPESWGGYH LIPRYFEFWQ GQSDRLHDRI VFERDVDVWL LKRLSP
