PDXS_STRCO
ID PDXS_STRCO Reviewed; 303 AA.
AC Q9L286;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SCO1523;
GN ORFNames=SCL2.13c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL939109; CAB70925.1; -; Genomic_DNA.
DR RefSeq; NP_625802.1; NC_003888.3.
DR RefSeq; WP_003977304.1; NZ_VNID01000021.1.
DR AlphaFoldDB; Q9L286; -.
DR SMR; Q9L286; -.
DR STRING; 100226.SCO1523; -.
DR GeneID; 1096949; -.
DR KEGG; sco:SCO1523; -.
DR PATRIC; fig|100226.15.peg.1532; -.
DR eggNOG; COG0214; Bacteria.
DR HOGENOM; CLU_055352_1_0_11; -.
DR InParanoid; Q9L286; -.
DR OMA; RYANRGW; -.
DR PhylomeDB; Q9L286; -.
DR UniPathway; UPA00245; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
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_0000109420"
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; 32202 MW; 0B179BC5B15074EA CRC64;
MSSTLSENQA PETGTARVKR GMAEQLKGGV IMDVVTPEQA KIAEDAGAVA VMALERVPAD
IRKDGGVARM SDPDMIEGII GAVSIPVMAK SRIGHFVEAQ VLQSLGVDYI DESEVLTPAD
EVNHSDKFAF TTPFVCGATN LGEALRRIAE GAAMIRSKGE AGTGNVVEAV RHLRQIKNEI
ARLRGYDNNE LYAAAKELRA PYELVKEVSE LGRLPVVLFS AGGVATPADA ALMRQLGAEG
VFVGSGIFKS GDPAKRAAAI VKATTFYDDP KIIADASRNL GEAMVGINCD TLPETERYAN
RGW
