ID   PDXS_CLOPA              Reviewed;          29 AA.
AC   P81356;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   02-JUN-2021, entry version 54.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824};
DE            Short=PLP synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824};
DE            EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01824};
DE   AltName: Full=Pdx1 {ECO:0000255|HAMAP-Rule:MF_01824};
DE   Flags: Fragment;
GN   Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824};
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=9629918; DOI=10.1002/elps.1150190533;
RA   Flengsrud R., Skjeldal L.;
RT   "Two-dimensional gel electrophoresis separation and N-terminal sequence
RT   analysis of proteins from Clostridium pasteurianum W5.";
RL   Electrophoresis 19:802-806(1998).
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 the PdxT subunit. Can also use ribulose 5-
CC       phosphate and dihydroxyacetone phosphate as substrates, resulting from
CC       enzyme-catalyzed isomerization of RBP and G3P, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_01824}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01824};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01824}.
CC   -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of heterodimers.
CC       {ECO:0000255|HAMAP-Rule:MF_01824}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown protein
CC       is 5.1, its MW is 32.7 kDa.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01824}.
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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   InterPro; IPR001852; PdxS/SNZ.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate; Schiff base.
FT   CHAIN           1..>29
FT                   /note="Pyridoxal 5'-phosphate synthase subunit PdxS"
FT                   /id="PRO_0000109387"
FT   VARIANT         26
FT                   /note="Q -> E"
FT   NON_TER         29
SQ   SEQUENCE   29 AA;  3155 MW;  4991308059BF3E75 CRC64;
     MGYDINXXLA QMXKGGVIMX XXXXXQAVI