PDXJ_CAMJE
ID PDXJ_CAMJE Reviewed; 257 AA.
AC Q9PN59; Q0P918;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00279};
DE Short=PNP synthase {ECO:0000255|HAMAP-Rule:MF_00279};
DE EC=2.6.99.2 {ECO:0000255|HAMAP-Rule:MF_00279};
GN Name=pdxJ {ECO:0000255|HAMAP-Rule:MF_00279}; OrderedLocusNames=Cj1238;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00279}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00279}.
CC -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00279}.
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DR EMBL; AL111168; CAL35353.1; -; Genomic_DNA.
DR PIR; H81330; H81330.
DR RefSeq; WP_002853163.1; NC_002163.1.
DR RefSeq; YP_002344629.1; NC_002163.1.
DR PDB; 3O6C; X-ray; 1.87 A; A=1-257.
DR PDB; 3O6D; X-ray; 1.95 A; A=1-257.
DR PDBsum; 3O6C; -.
DR PDBsum; 3O6D; -.
DR AlphaFoldDB; Q9PN59; -.
DR SMR; Q9PN59; -.
DR IntAct; Q9PN59; 25.
DR STRING; 192222.Cj1238; -.
DR PaxDb; Q9PN59; -.
DR PRIDE; Q9PN59; -.
DR EnsemblBacteria; CAL35353; CAL35353; Cj1238.
DR GeneID; 905529; -.
DR KEGG; cje:Cj1238; -.
DR PATRIC; fig|192222.6.peg.1220; -.
DR eggNOG; COG0854; Bacteria.
DR HOGENOM; CLU_074563_0_0_7; -.
DR OMA; SNAGWDT; -.
DR UniPathway; UPA00244; UER00313.
DR EvolutionaryTrace; Q9PN59; -.
DR Proteomes; UP000000799; 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; -; 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 PANTHER; PTHR30456; PTHR30456; 1.
DR Pfam; PF03740; PdxJ; 1.
DR SUPFAM; SSF63892; SSF63892; 1.
DR TIGRFAMs; TIGR00559; pdxJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pyridoxine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..257
FT /note="Pyridoxine 5'-phosphate synthase"
FT /id="PRO_0000190111"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 6
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00279"
FT BINDING 17
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 43
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 48
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 98
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 211
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 232..233
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT SITE 147
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 178..201
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3O6C"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3O6C"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:3O6C"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:3O6C"
SQ SEQUENCE 257 AA; 29011 MW; 19C480DA3B96012F CRC64;
MLLGVNIDHI AVLRQARMVN DPDLLEAAFI VARHGDQITL HVREDRRHAQ DFDLENIIKF
CKSPVNLECA LNDEILNLAL KLKPHRVTLV PEKREELTTE GGLCLNHAKL KQSIEKLQNA
NIEVSLFINP SLEDIEKSKI LKAQFIELHT GHYANLHNAL FSNISHTAFA LKELDQDKKT
LQAQFEKELQ NLELCAKKGL ELGLKVAAGH GLNYKNVKPV VKIKEICELN IGQSIVARSV
FTGLQNAILE MKELIKR
