ID   PDXS_MYCPA              Reviewed;         303 AA.
AC   Q73WF0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
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};
GN   Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824}; OrderedLocusNames=MAP_2710c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01824}.
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DR   EMBL; AE016958; AAS05027.1; -; Genomic_DNA.
DR   RefSeq; WP_003878553.1; NC_002944.2.
DR   AlphaFoldDB; Q73WF0; -.
DR   SMR; Q73WF0; -.
DR   STRING; 262316.MAP_2710c; -.
DR   EnsemblBacteria; AAS05027; AAS05027; MAP_2710c.
DR   GeneID; 66694721; -.
DR   KEGG; mpa:MAP_2710c; -.
DR   eggNOG; COG0214; Bacteria.
DR   HOGENOM; CLU_055352_1_0_11; -.
DR   OMA; RYANRGW; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome; Schiff base.
FT   CHAIN           1..303
FT                   /note="Pyridoxal 5'-phosphate synthase subunit PdxS"
FT                   /id="PRO_0000109404"
FT   ACT_SITE        90
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         33
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         162
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         174
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         223
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         244..245
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
SQ   SEQUENCE   303 AA;  31964 MW;  8F1F082A3B09C08D CRC64;
     MNTAHSPDGS GRTGTARVKR GMAEMLKGGV IMDVVTPEQA KIAEGAGAVA VMALERVPAD
     IRAQGGVSRM SDPDMIEGII SAVTIPVMAK ARIGHFVEAQ ILQSLGVDYI DESEVLTPAD
     YTHHIDKWKF TVPFVCGATN LGEALRRINE GAAMIRSKGE AGTGDVSNAT THMRAIGGEI
     RRLMSLSEDE LYVAAKELQA PYELVVEVAR AGKLPVTLFT AGGIATPADA AMMMQLGAEG
     VFVGSGIFKS GDPAQRAAAI VKATTFYDDP DVLAKVSRGL GEAMVGINVE QIAQPERLAE
     RGW