PDXH_PSYA2
ID PDXH_PSYA2 Reviewed; 216 AA.
AC Q4FS02;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Psyc_1358;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19206.1; -; Genomic_DNA.
DR RefSeq; WP_011280627.1; NC_007204.1.
DR AlphaFoldDB; Q4FS02; -.
DR SMR; Q4FS02; -.
DR STRING; 259536.Psyc_1358; -.
DR EnsemblBacteria; AAZ19206; AAZ19206; Psyc_1358.
DR KEGG; par:Psyc_1358; -.
DR eggNOG; COG0259; Bacteria.
DR HOGENOM; CLU_032263_2_2_6; -.
DR OMA; PEPNAMV; -.
DR OrthoDB; 1542844at2; -.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR Proteomes; UP000000546; 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..216
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT /id="PRO_0000167742"
FT BINDING 9..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 62..67
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 77..78
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 142..143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 198
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ SEQUENCE 216 AA; 24642 MW; 9C9E6B4BD8385764 CRC64;
MNMDFTDQRL SYEKGQLDQQ SVPISPFELL KAWMHEAIEE QVQEPYAMSL ATCGADDKPS
VRIVLLREIT DKGIVFYTNY ESAKGQDIAE NPNAEALFFW HKLERQIRIS GSIAKIDADK
SAAYFQKRPH DSQVGTWVSQ PQSGEVASRD VMEQTFEQLQ TDYPDGAAVP TPGFWGGYEI
TVSEIEFWQG RANRMHDRIV YHKEVDGSFS TKRLLP
