ID A0A6N1L0B5_ACILW Unreviewed; 219 AA. AC A0A6N1L0B5; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 22-FEB-2023, entry version 11. DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000256|HAMAP-Rule:MF_01629}; DE EC=1.4.3.5 {ECO:0000256|HAMAP-Rule:MF_01629}; DE AltName: Full=PNP/PMP oxidase {ECO:0000256|HAMAP-Rule:MF_01629}; DE Short=PNPOx {ECO:0000256|HAMAP-Rule:MF_01629}; DE AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01629}; GN Name=pdxH {ECO:0000256|HAMAP-Rule:MF_01629, GN ECO:0000313|EMBL:QKT98680.1}; GN ORFNames=FOB20_07605 {ECO:0000313|EMBL:QKT98680.1}; OS Acinetobacter lwoffii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter. OX NCBI_TaxID=28090 {ECO:0000313|EMBL:QKT98680.1, ECO:0000313|Proteomes:UP000509137}; RN [1] {ECO:0000313|EMBL:QKT98680.1, ECO:0000313|Proteomes:UP000509137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_551 {ECO:0000313|EMBL:QKT98680.1, RC ECO:0000313|Proteomes:UP000509137}; RA Patel R., Rucinski S., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A., RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (NOV-2019) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01629}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01629, CC ECO:0000256|PIRSR:PIRSR000190-2}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01629, CC ECO:0000256|PIRSR:PIRSR000190-2}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01629}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01629}. CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family. CC {ECO:0000256|ARBA:ARBA00007301, ECO:0000256|HAMAP-Rule:MF_01629}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP054822; QKT98680.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6N1L0B5; -. DR UniPathway; UPA01068; UER00304. DR Proteomes; UP000509137; 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 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; 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 TIGRFAMs; TIGR00558; pdxH; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. PE 3: Inferred from homology; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_01629}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01629}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01629}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629}. FT DOMAIN 40..124 FT /note="Pyridoxamine 5'-phosphate oxidase putative" FT /evidence="ECO:0000259|Pfam:PF01243" FT DOMAIN 179..219 FT /note="Pyridoxine 5'-phosphate oxidase dimerisation C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF10590" FT BINDING 13..16 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 66..71 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629" FT BINDING 71 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 81..82 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" FT BINDING 88 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" FT BINDING 110 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 146..147 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" FT BINDING 192 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" FT BINDING 198..200 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-1" FT BINDING 202 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01629, FT ECO:0000256|PIRSR:PIRSR000190-2" SQ SEQUENCE 219 AA; 25931 MW; 6BA2D332E21EAB4A CRC64; MMSDLIKDLS ELRLNYEKGE LQEQQVNPNP HMQFLQWFNH ALEAKLHEPY AMSLATANAQ GRPHVRTVLL RGATEAGYDF YTNYDSQKGL DLAENPYAEL LLYWQDQERQ IRISGRVKKI SEEESTDYYH KRPRESQIAA HISTPQSGIV ASREELQQRF WDLHTQVANQ QELDKPIFWG GYRLEPDYYE FWQGRPNRLH DRLSYRKTDA GWTLERLMP //