PDXH1_HYDCU
ID PDXH1_HYDCU Reviewed; 216 AA.
AC Q31IR4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase 1 {ECO:0000255|HAMAP-Rule:MF_01629};
DE EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629};
DE AltName: Full=PNP/PMP oxidase 1 {ECO:0000255|HAMAP-Rule:MF_01629};
DE Short=PNPOx 1 {ECO:0000255|HAMAP-Rule:MF_01629};
DE AltName: Full=Pyridoxal 5'-phosphate synthase 1 {ECO:0000255|HAMAP-Rule:MF_01629};
GN Name=pdxH1 {ECO:0000255|HAMAP-Rule:MF_01629}; OrderedLocusNames=Tcr_0363;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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; CP000109; ABB40959.1; -; Genomic_DNA.
DR RefSeq; WP_011369784.1; NC_007520.2.
DR AlphaFoldDB; Q31IR4; -.
DR SMR; Q31IR4; -.
DR STRING; 317025.Tcr_0363; -.
DR EnsemblBacteria; ABB40959; ABB40959; Tcr_0363.
DR KEGG; tcx:Tcr_0363; -.
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 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..216
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase 1"
FT /id="PRO_0000255894"
FT BINDING 10..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 63..68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 78..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 133
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 186
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 192..194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 196
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ SEQUENCE 216 AA; 25160 MW; 31FFE39B0E9EFD58 CRC64;
MPNRDYHAER REYGFAALRR ADLQTDPFHQ FSDWMETALE KTQQDATAMS VSTVSADGQP
HSRIVLLKTF NSDGFIFYTH YDSDKGQQID QNAKAALLFF WPELDRQIRI EGSLQKVPRE
TSEAYFHSRP KDSQLAASIS NQSQPVASRD ILEAKLQEAM SLPDRNLTCP AHWGGYQLKP
CYFEFWQGRP SRLHDRFRYQ RLSKNDQAWQ ITRLNP
