PDXJ_PSEAB
ID PDXJ_PSEAB Reviewed; 248 AA.
AC Q02HS5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=PA14_54290;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ09925.1; -; Genomic_DNA.
DR RefSeq; WP_003101974.1; NZ_CP034244.1.
DR PDB; 5DLC; X-ray; 2.65 A; A/B/C/D=1-248.
DR PDBsum; 5DLC; -.
DR AlphaFoldDB; Q02HS5; -.
DR SMR; Q02HS5; -.
DR PRIDE; Q02HS5; -.
DR EnsemblBacteria; ABJ09925; ABJ09925; PA14_54290.
DR KEGG; pau:PA14_54290; -.
DR HOGENOM; CLU_074563_0_0_6; -.
DR OMA; SNAGWDT; -.
DR BioCyc; PAER208963:G1G74-4571-MON; -.
DR UniPathway; UPA00244; UER00313.
DR Proteomes; UP000000653; 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; Transferase.
FT CHAIN 1..248
FT /note="Pyridoxine 5'-phosphate synthase"
FT /id="PRO_1000022391"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 12
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 14..15
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 23
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 50
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 55
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 105
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 197
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT BINDING 218..219
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT SITE 156
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:5DLC"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:5DLC"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5DLC"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:5DLC"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5DLC"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:5DLC"
SQ SEQUENCE 248 AA; 27260 MW; E7FF4496D6F3E605 CRC64;
MTEATRILLG VNIDHVATLR QARGTRYPDP VKAALDAEEA GADGITVHLR EDRRHIQERD
VRVLKEVLQT RMNFEMGVTE EMLAFAEEIR PAHSCLVPER REELTTEGGL DVAGQEQRIR
DAVRRLAAVG SEVSLFIDPD PRQIEASARV GAPAIELHTG RYADAEDPEE QARELQRVRE
GVALGRSLGL IVNAGHGLHY HNVEPVAAID GINELNIGHA IVAHALFVGF RQAVAEMKAL
MLAAATKR
