ID C5ZV09_9HELI Unreviewed; 259 AA.
AC C5ZV09;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:EES88823.1};
GN ORFNames=HCAN_0099 {ECO:0000313|EMBL:EES88823.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES88823.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES88823.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
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; CM000776; EES88823.1; -; Genomic_DNA.
DR RefSeq; WP_006656679.1; NZ_CM000776.2.
DR AlphaFoldDB; C5ZV09; -.
DR STRING; 537970.HCAN_0099; -.
DR eggNOG; COG0854; Bacteria.
DR HOGENOM; CLU_074563_0_0_7; -.
DR OrthoDB; 9806590at2; -.
DR UniPathway; UPA00244; UER00313.
DR Proteomes; UP000007032; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW 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 213
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 214
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 235..236
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 259 AA; 28873 MW; 1AD3C7FE08D14F80 CRC64;
MLLGVNIDHI ATLREARKIN DPDPLEAIFI AKRAGADQIT MHLREDRRHM HDEDILRIAQ
SSFLPINIES SINPTIIEFL LKIAPHRITL VPENREEVTT EGGLNVVGNF ERILQITKSF
QEVGTQVSLF IDSEASQIEA SKEVGAEMIE LHTGSYANLH LMLFSNLPKM KNSIKELELP
KKELLGLWEQ SLESLKKGAK KANELGLGVA AGHGLNYVNL KPILEIQEIV ELNIGQSIIA
RAIFVGLENA IRELKALLV
//
