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Database: UniProt
Entry: D2QCW2_SPILD
LinkDB: D2QCW2_SPILD
Original site: D2QCW2_SPILD 
ID   D2QCW2_SPILD            Unreviewed;       245 AA.
AC   D2QCW2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE            Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE            EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279};
GN   Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279};
GN   OrderedLocusNames=Slin_4990 {ECO:0000313|EMBL:ADB40968.1};
OS   Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896 / Claus 1).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB40968.1, ECO:0000313|Proteomes:UP000002028};
RN   [1] {ECO:0000313|Proteomes:UP000002028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC   {ECO:0000313|Proteomes:UP000002028};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA   Goker M., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Spirosoma linguale DSM 74.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADB40968.1, ECO:0000313|Proteomes:UP000002028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC   {ECO:0000313|Proteomes:UP000002028};
RX   PubMed=21304700;
RA   Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA   Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M.,
RA   Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.;
RT   "Complete genome sequence of Spirosoma linguale type strain (1).";
RL   Stand. Genomic Sci. 2:176-185(2010).
CC   -!- FUNCTION: Catalyzes the complicated ring closure reaction between the
CC       two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-
CC       2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form
CC       pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate
CC         = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate;
CC         Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58589; EC=2.6.99.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00279};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
CC       {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00279}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00279}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00279}.
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DR   EMBL; CP001769; ADB40968.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2QCW2; -.
DR   STRING; 504472.Slin_4990; -.
DR   KEGG; sli:Slin_4990; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_1_0_10; -.
DR   OMA; SNAGWDT; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000002028; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00003; PNPsynthase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00279; PdxJ; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004569; PyrdxlP_synth_PdxJ.
DR   InterPro; IPR036130; Pyridoxine-5'_phos_synth.
DR   NCBIfam; TIGR00559; pdxJ; 1.
DR   PANTHER; PTHR30456; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR30456:SF0; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; Pyridoxine 5'-phosphate synthase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00279};
KW   Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW   Rule:MF_00279};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000313|EMBL:ADB40968.1}.
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         7
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         18
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         45
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         50
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         100
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         191
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         213..214
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   SITE            151
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   245 AA;  27218 MW;  3A68D81A83CBA769 CRC64;
     MTRLSVNINK IATIRNARGG NNPDLVKVAL DCERFGAQGI TVHPRPDERH IRYQDVLDLH
     EVVTTEFNIE GNPDERFIEL VKRVKPAQVT LVPDAVDAIT SNAGWDTIRH ADHLRKLVDT
     FKADGIRVSI FVDADERMVE GAKAVGTDRI ELYTEPYAAH YAENREAAVA PFVRAAQRAN
     QLGLGLNAGH DLSLENLRFF DEQVPGLEEV SIGHALVCDA LYFGLENTIQ MYLRCLDRTG
     GPAGF
//
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