(data stored in SCRATCH zone)

SWISSPROT: D4YYR9_SPHJU

ID   D4YYR9_SPHJU            Unreviewed;       245 AA.
AC   D4YYR9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00088558};
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:SAAS00088588};
GN   Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279,
GN   ECO:0000313|EMBL:BAI95501.1};
GN   OrderedLocusNames=SJA_C1-06670 {ECO:0000313|EMBL:BAI95501.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95501.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95501.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:SAAS00384571}.
CC   -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-
CC       oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2
CC       H(2)O. {ECO:0000256|HAMAP-Rule:MF_00279,
CC       ECO:0000256|SAAS:SAAS00384586}.
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:SAAS00384576}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00279, ECO:0000256|SAAS:SAAS00088573}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
CC       ECO:0000256|SAAS:SAAS00384544}.
CC   -!- SIMILARITY: Belongs to the PNP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00571308}.
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DR   EMBL; AP010803; BAI95501.1; -; Genomic_DNA.
DR   RefSeq; WP_007686507.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06670; -.
DR   EnsemblBacteria; BAI95501; BAI95501; SJA_C1-06670.
DR   GeneID; 29272340; -.
DR   KEGG; sjp:SJA_C1-06670; -.
DR   eggNOG; ENOG4105CSZ; Bacteria.
DR   eggNOG; COG0854; LUCA.
DR   HOGENOM; HOG000258094; -.
DR   KO; K03474; -.
DR   OMA; TSNAGWD; -.
DR   OrthoDB; POG091H03D1; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
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   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; SSF63892; 1.
DR   TIGRFAMs; TIGR00559; pdxJ; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYR9.
DR   SWISS-2DPAGE; D4YYR9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00088560};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00088577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00279,
KW   ECO:0000256|SAAS:SAAS00461397, ECO:0000313|EMBL:BAI95501.1}.
FT   REGION       15     16       1-deoxy-D-xylulose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   REGION      218    219       3-amino-2-oxopropyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   ACT_SITE     49     49       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   ACT_SITE     76     76       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   BINDING      13     13       3-amino-2-oxopropyl phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      24     24       3-amino-2-oxopropyl phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      51     51       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING      56     56       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING     106    106       1-deoxy-D-xylulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   BINDING     197    197       3-amino-2-oxopropyl phosphate; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00279}.
FT   SITE        157    157       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00279}.
SQ   SEQUENCE   245 AA;  26177 MW;  155709CA5022E1E2 CRC64;
     MSRTPAHLRL GVNIDHVATI RNARGGTHPD PVKAALLAAK AGADGITAHL REDRRHIRDE
     DIATLMAALT VPLNLEMAAT QEMLGIALRH RPHAACIVPE KREERTTEGG LDAAGQIDAL
     HPIVDALGKA GVRVSLFIEP DAAQIEAAMR LGAPVVELHT GRYAHLEGSE RAEELRRLAD
     AAALAAKNGI EPHAGHGLTF DNVGPVAAIP QIAELNIGHF LIGEAIFGGL ESSIREMRRQ
     MDLAR
//

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