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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
 
 
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