(data stored in ACNUC7421 zone)

SWISSPROT: B4SR18_STRM5

ID   B4SR18_STRM5            Unreviewed;       247 AA.
AC   B4SR18;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958133};
DE            Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE            EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958138};
GN   Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279};
GN   OrderedLocusNames=Smal_0014 {ECO:0000313|EMBL:ACF49719.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49719.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49719.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49719.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the complicated ring closure reaction between
CC       the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and
CC       3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP)
CC       to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl
CC         phosphate = 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, ECO:0000256|SAAS:SAAS01116070};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00279,
CC       ECO:0000256|SAAS:SAAS00958122}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00279, ECO:0000256|SAAS:SAAS00958137}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
CC       ECO:0000256|SAAS:SAAS00958140}.
CC   -!- SIMILARITY: Belongs to the PNP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958135}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00279}.
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DR   EMBL; CP001111; ACF49719.1; -; Genomic_DNA.
DR   RefSeq; WP_004132724.1; NC_011071.1.
DR   STRING; 391008.Smal_0014; -.
DR   EnsemblBacteria; ACF49719; ACF49719; Smal_0014.
DR   KEGG; smt:Smal_0014; -.
DR   eggNOG; ENOG4105CSZ; Bacteria.
DR   eggNOG; COG0854; LUCA.
DR   HOGENOM; HOG000258095; -.
DR   KO; K03474; -.
DR   OMA; TSNAGWD; -.
DR   OrthoDB; 1159993at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00070-MONOMER; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000001867; 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; -; 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   PANTHER; PTHR30456; PTHR30456; 1.
DR   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; SSF63892; 1.
DR   TIGRFAMs; TIGR00559; pdxJ; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SR18.
DR   SWISS-2DPAGE; B4SR18.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00958134};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00958120};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00958119}.
FT   REGION      224    225       3-amino-2-oxopropyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   ACT_SITE     43     43       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   ACT_SITE     73     73       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   ACT_SITE    201    201       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   BINDING       7      7       3-amino-2-oxopropyl phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      18     18       3-amino-2-oxopropyl phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      45     45       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      50     50       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING     110    110       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING     202    202       3-amino-2-oxopropyl phosphate; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   SITE        161    161       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
SQ   SEQUENCE   247 AA;  26163 MW;  03BBB0DD7801A55D CRC64;
     MTQLSVNVNK IAVLRNSRGG AEPDVVRAAQ ACLDAGAHGI TVHPRPDRRH ITAEDVLALS
     TLTRARGVEF NIEGNPFAPP REGYPGLLPL CAQTRPAQAT LVPDSDGQIT SDHGFDFERD
     AERLRPLIAE LKAMGCRVSL FVDAGNPLLE QAAEVGADRI ELYTGPYAEA HAAGDAGAML
     TLFATAARRA QAVGLGVNAG HDLSQDNLRD FLANVPDVLE VSIGHALIGE ALYDGLDATV
     RGYLALL
//

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