ID   PDX1_HEVBR              Reviewed;         309 AA.
AC   Q39963;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable pyridoxal 5'-phosphate synthase subunit PDX1;
DE            Short=PLP synthase subunit PDX1;
DE            EC=4.3.3.6;
DE   AltName: Full=Ethylene-inducible protein HEVER;
GN   Name=PDX1; Synonyms=ER1;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   TISSUE=Laticifer;
RX   PubMed=7579163; DOI=10.1007/bf00019129;
RA   Sivasubramaniam S., Vanniasingham V.M., Tan C.T., Chua N.H.;
RT   "Characterisation of HEVER, a novel stress-induced gene from Hevea
RT   brasiliensis.";
RL   Plant Mol. Biol. 29:173-178(1995).
CC   -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose
CC       5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The
CC       ammonia is provided by PDX2. Can also use ribulose 5-phosphate and
CC       dihydroxyacetone phosphate as substrates, resulting from enzyme-
CC       catalyzed isomerization of RBP and G3P, respectively. Also plays an
CC       indirect role in resistance to singlet oxygen-generating
CC       photosensitizers. {ECO:0000250|UniProtKB:O80448}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC         ChEBI:CHEBI:597326; EC=4.3.3.6;
CC         Evidence={ECO:0000250|UniProtKB:Q03148};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC   -!- INDUCTION: By stress treatment with salicylic acid and ethephon.
CC       {ECO:0000269|PubMed:7579163}.
CC   -!- MISCELLANEOUS: Vitamin B6 is an essential quencher of singlet oxygen in
CC       plants, that can protect cellular membranes from lipid peroxidation.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000305}.
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DR   EMBL; M88254; AAA91063.1; -; mRNA.
DR   PIR; S60047; S60047.
DR   PIR; S71492; S71492.
DR   AlphaFoldDB; Q39963; -.
DR   SMR; Q39963; -.
DR   OrthoDB; 1090029at2759; -.
DR   UniPathway; UPA00245; -.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04727; pdxS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01824; PdxS; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001852; PdxS/SNZ.
DR   InterPro; IPR033755; PdxS/SNZ_N.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR31829; PTHR31829; 1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00343; TIGR00343; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Schiff base; Stress response.
FT   CHAIN           1..309
FT                   /note="Probable pyridoxal 5'-phosphate synthase subunit
FT                   PDX1"
FT                   /id="PRO_0000109371"
FT   ACT_SITE        97
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         40
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         169
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         181
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:Q03148"
FT   BINDING         230
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         251..252
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
SQ   SEQUENCE   309 AA;  33133 MW;  AA38867583905403 CRC64;
     MAGTGVVAVY GNGAITETKK SPFSVKVGLA QMLRGGVIMD VVNPEQARIA EEAGACAVMA
     LERVPADIRA QGGVARMSDP QLIKEIKQSV TIPVMAKARI GHFVEAQILE AIGIDYVDES
     EVLTPADEEN HINKHNFRIP FVCGCRNLGE ALRRIREGAA MIRTKGEAGT GNVIEAVRHV
     RSVMGDIRLL RNMDDDEVFT FAKKIAAPYD LVMQTKQLGR LPVVQFAAGG VATPADAALM
     MQLGCDGVFV GSGVFKSGDP ARRARAIVQA VTHYSDPDML AEVSCGLGEA MVGINLNDKK
     VERFANRSE