ID PDXH_KINRD Reviewed; 223 AA. AC A6WE21; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 02-DEC-2020, entry version 79. DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629}; GN Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629}; OrderedLocusNames=Krad_3597; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216). OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus. OX NCBI_TaxID=266940; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., RA Fliermans C., Richardson P.; RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate CC (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}. 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:0000255|HAMAP-Rule:MF_01629}; 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:0000255|HAMAP-Rule:MF_01629}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01629}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000750; ABS05060.1; -; Genomic_DNA. DR RefSeq; WP_012086678.1; NC_009664.2. DR SMR; A6WE21; -. DR STRING; 266940.Krad_3597; -. DR EnsemblBacteria; ABS05060; ABS05060; Krad_3597. DR KEGG; kra:Krad_3597; -. DR eggNOG; COG0259; Bacteria. DR HOGENOM; CLU_032263_2_2_11; -. DR OMA; PEPNAMV; -. DR OrthoDB; 1542844at2; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000001116; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-UniRule. 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..223 FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase" FT /id="PRO_0000335788" FT NP_BIND 60..65 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT NP_BIND 75..76 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT NP_BIND 139..140 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT REGION 8..11 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT REGION 194..196 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 65 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 81 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 82 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 104 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 122 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 126 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 130 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 188 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 198 FT /note="FMN" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" SQ SEQUENCE 223 AA; 24864 MW; A8EE8EF8CC392AE8 CRC64; MEDPAGRRVD YGDRRFDEHD LAPTPLAQFQ AWYSDAVEAG VVEPNAMTVA TAGADGVSAR TVLLKAVDGR GFVFYTNQRS RKALAIAHDP RVALLFTWHG THRQVAVRGT AEEVPRAETE AYFASRPYGS RIGAWVSEQS RTTPSAAALH EREAQLRERW PDTGSPDDVP TPPHWGGYLV RALEVEFWQG RTSRLHDRLV LVAADGPARL DDPAPWRTER RQP //