ID X5EU15_NEIME Unreviewed; 242 AA.
AC X5EU15;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279};
GN Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279,
GN ECO:0000313|EMBL:AHW76559.1};
GN ORFNames=NMA510612_2293 {ECO:0000313|EMBL:AHW76559.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:AHW76559.1, ECO:0000313|Proteomes:UP000023582};
RN [1] {ECO:0000313|EMBL:AHW76559.1, ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RX PubMed=24812217;
RA Zhang Y., Yang J., Xu L., Zhu Y., Liu B., Shao Z., Zhang X., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitidis Serogroup A Strain
RT NMA510612, Isolated from a Patient with Bacterial Meningitis in China.";
RL Genome Announc. 2:e00360-14(2014).
RN [2] {ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RA Zhang X., Zhang Y., Yang J., Zhu Y., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitides, serogroup A strain
RT 510612.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the complicated ring closure reaction between the
CC two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-
CC 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form
CC pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate
CC = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate;
CC Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:58589; EC=2.6.99.2; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00279};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
CC {ECO:0000256|HAMAP-Rule:MF_00279}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_00279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279}.
CC -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000256|HAMAP-
CC Rule:MF_00279}.
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DR EMBL; CP007524; AHW76559.1; -; Genomic_DNA.
DR RefSeq; WP_002229055.1; NZ_VALL01000067.1.
DR SMR; X5EU15; -.
DR GeneID; 61281950; -.
DR KEGG; nmx:NMA510612_2293; -.
DR PATRIC; fig|487.517.peg.2264; -.
DR UniPathway; UPA00244; UER00313.
DR Proteomes; UP000023582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00003; PNPsynthase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00279; PdxJ; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004569; PyrdxlP_synth_PdxJ.
DR InterPro; IPR036130; Pyridoxine-5'_phos_synth.
DR NCBIfam; TIGR00559; pdxJ; 1.
DR PANTHER; PTHR30456; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR30456:SF0; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF03740; PdxJ; 1.
DR SUPFAM; SSF63892; Pyridoxine 5'-phosphate synthase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00279};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_00279}; Transferase {ECO:0000256|HAMAP-Rule:MF_00279}.
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 6
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 8..9
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 17
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 44
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 49
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 99
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 191
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 212..213
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT SITE 150
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ SEQUENCE 242 AA; 26670 MW; 07AC9E95DDA8D090 CRC64;
MLLGVNIDHI ATVRNARGTT YPSPVEAALV AETHGADLIT MHLREDRRHI KDADVFAVKN
AIRTRLNLEM ALTEEMLENA LKVMPEDVCI VPEKRQEITT EGGLDVLAQQ DKIAEFTKIL
TDAGIRVSLF IDADDRQIQA ARDVGAPVVE LHTGAYADAR SHAEQIRQFE RIQNGAHFAS
DLGLVVNAGH GLTIHNVTPI AQILAIRELN IGHSLISQAL FLGLPEAVRQ MKEAMFRARL
LP
//
