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 28-FEB-2018, entry version 70. 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}; GN OrderedLocusNames=Krad_3597; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / OS SRS30216). OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; OC 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., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., RA Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., RA Shimkets L., Berry C.J., Fliermans C., Richardson P.; RT "Complete sequence of chromosome of Kineococcus radiotolerans RT SRS30216."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- CC phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal CC 5'-phosphate (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) = CC pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000255|HAMAP- CC Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'- CC phosphate + H(2)O(2). {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; CC pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 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 CC family. {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 ProteinModelPortal; A6WE21; -. DR SMR; A6WE21; -. DR STRING; 266940.Krad_3597; -. DR EnsemblBacteria; ABS05060; ABS05060; Krad_3597. DR KEGG; kra:Krad_3597; -. DR eggNOG; ENOG4108S7T; Bacteria. DR eggNOG; COG0259; LUCA. DR HOGENOM; HOG000242755; -. DR KO; K00275; -. DR OMA; PEPNAMV; -. DR OrthoDB; POG091H054N; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000001116; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-EC. 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:SF0; PTHR10851:SF0; 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 Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Pyridoxine biosynthesis; Reference proteome. FT CHAIN 1 223 Pyridoxine/pyridoxamine 5'-phosphate FT oxidase. FT /FTId=PRO_0000335788. FT NP_BIND 60 65 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 75 76 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 139 140 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT REGION 8 11 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT REGION 194 196 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 81 81 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 82 82 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 104 104 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 126 126 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 130 130 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 188 188 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 198 198 FMN. {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 //