ID   PDX1_STELP              Reviewed;         235 AA.
AC   Q41348;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=H47;
DE   Flags: Fragment;
OS   Stellaria longipes (Longstalk starwort) (Alsine longipes).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Alsineae; Stellaria.
OX   NCBI_TaxID=19744;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Zhang X.-H.;
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA50602.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X71601; CAA50602.1; ALT_INIT; mRNA.
DR   PIR; S33204; S33204.
DR   AlphaFoldDB; Q41348; -.
DR   SMR; Q41348; -.
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   Gene3D; 3.20.20.70; -; 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   SUPFAM; SSF51366; SSF51366; 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.
FT   CHAIN           <1..235
FT                   /note="Probable pyridoxal 5'-phosphate synthase subunit
FT                   PDX1"
FT                   /id="PRO_0000109373"
FT   ACT_SITE        16
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         104
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:Q03148"
FT   BINDING         153
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         174..175
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   NON_TER         1
SQ   SEQUENCE   235 AA;  25450 MW;  7009E5A53E2D0E0C CRC64;
     LIKEIKAAVT IPVMAKARIG HFVEAQILES IGVDYVDESE VLTPADEDHH INKHNFQIPF
     VCGLSIPRGA PPPAYRRGYA GHDTGPRVRK PSTGNVVEAV RHIRSVMGEI RLLRNMDDDE
     VFAYAKKISA AYDLVMQTKQ LGRLPVVNFA AGGVATPADA ALMMQLGCDG VFVGSGVFKS
     GDPAKRARAI VQAVTHYSDP DLLGRGEFGL GEAMVGIIVR MRRLRGTPIV LNEVI