PDXH_ACIBS
ID PDXH_ACIBS Reviewed; 218 AA.
AC B0VNC8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=ABSDF3447;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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}.
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DR EMBL; CU468230; CAP02714.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VNC8; -.
DR SMR; B0VNC8; -.
DR EnsemblBacteria; CAP02714; CAP02714; ABSDF3447.
DR KEGG; abm:ABSDF3447; -.
DR HOGENOM; CLU_032263_2_2_6; -.
DR OMA; PEPNAMV; -.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR Proteomes; UP000001741; 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.
FT CHAIN 1..218
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT /id="PRO_1000186281"
FT BINDING 12..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 65..70
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 80..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 145..146
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 191
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 197..199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 201
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ SEQUENCE 218 AA; 25481 MW; 7C14DA88800D9267 CRC64;
MSDVIKDLSE LRLSYEQGEL YETQVASNPH EQFLGWFNHA LAANLHEPYA MSLATASASG
RPHVRTVLLR GATEAGYDFY TNYDSQKGID LAENPYAELL FYWPSLERQV RVGGHVVKIP
EQESTDYYHK RPRDSQIAAY ISTPQSGKIE SRELLQQRFQ DLQQQVQSHE VLDKPEFWGG
YRLQPDYYEF WQGRPNRLHD RLSYEKIDGQ WTLHRLMP
