PDXH_MYCTO
ID PDXH_MYCTO Reviewed; 224 AA.
AC P9WIJ0; L0TBR8; O06207; P65682;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=MT2682;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC (PLP). {ECO:0000250, 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:0000250, ECO:0000255|HAMAP-Rule:MF_01629};
CC Note=Binds 1 FMN per subunit. {ECO:0000250, ECO:0000255|HAMAP-
CC 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:0000250, ECO:0000255|HAMAP-Rule:MF_01629}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000255|HAMAP-Rule:MF_01629, ECO:0000305}.
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DR EMBL; AE000516; AAK46998.1; -; Genomic_DNA.
DR PIR; F70570; F70570.
DR RefSeq; WP_003413471.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIJ0; -.
DR SMR; P9WIJ0; -.
DR EnsemblBacteria; AAK46998; AAK46998; MT2682.
DR GeneID; 45426610; -.
DR KEGG; mtc:MT2682; -.
DR PATRIC; fig|83331.31.peg.2892; -.
DR HOGENOM; CLU_032263_2_2_11; -.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR Proteomes; UP000001020; 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..224
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT /id="PRO_0000427998"
FT BINDING 19..22
FT /ligand="substrate"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 76..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 91..92
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 155..156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250, 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"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01629"
FT BINDING 211
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ SEQUENCE 224 AA; 25186 MW; 66ABC0AAACE90DC1 CRC64;
MDDDAQMVAI DKDQLARMRG EYGPEKDGCG DLDFDWLDDG WLTLLRRWLN DAQRAGVSEP
NAMVLATVAD GKPVTRSVLC KILDESGVAF FTSYTSAKGE QLAVTPYASA TFPWYQLGRQ
AHVQGPVSKV STEEIFTYWS MRPRGAQLGA WASQQSRPVG SRAQLDNQLA EVTRRFADQD
QIPVPPGWGG YRIAPEIVEF WQGRENRMHN RIRVANGRLE RLQP
