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Database: UniProt/TrEMBL
Entry: G0BHK1_9ENTR
LinkDB: G0BHK1_9ENTR
Original site: G0BHK1_9ENTR 
ID   G0BHK1_9ENTR            Unreviewed;       243 AA.
AC   G0BHK1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   11-JUN-2014, entry version 18.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase;
DE            Short=PNP synthase;
DE            EC=2.6.99.2;
GN   Name=pdxJ; ORFNames=SerAS12_3858;
OS   Serratia sp. AS12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Serratia.
OX   NCBI_TaxID=768490;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AS12;
RX   PubMed=22768360; DOI=10.4056/sigs.2705996;
RA   Neupane S., Finlay R.D., Alstrom S., Goodwin L., Kyrpides N.C.,
RA   Lucas S., Lapidus A., Bruce D., Pitluck S., Peters L.,
RA   Ovchinnikova G., Chertkov O., Han J., Han C., Tapia R., Detter J.C.,
RA   Land M., Hauser L., Cheng J.F., Ivanova N., Pagani I., Klenk H.P.,
RA   Woyke T., Hogberg N.;
RT   "Complete genome sequence of Serratia plymuthica strain AS12.";
RL   Stand. Genomic Sci. 6:165-173(2012).
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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-
CC       oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2
CC       H(2)O.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 5/5.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PNP synthase family.
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DR   EMBL; CP002774; AEF51910.1; -; Genomic_DNA.
DR   RefSeq; YP_004502267.1; NC_015566.1.
DR   EnsemblBacteria; AEF51910; AEF51910; SerAS12_3858.
DR   GeneID; 10627995; -.
DR   KEGG; srs:SerAS12_3858; -.
DR   KO; K03474; -.
DR   BioCyc; SSP768490:GH4I-3940-MONOMER; -.
DR   UniPathway; UPA00244; UER00313.
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   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;
KW   Complete proteome; Cytoplasm; Pyridoxine biosynthesis; Transferase.
FT   REGION       11     12       1-deoxy-D-xylulose 5-phosphate binding
FT                                (By similarity).
FT   REGION      215    216       3-amino-2-oxopropyl phosphate binding (By
FT                                similarity).
FT   ACT_SITE     45     45       Proton acceptor (By similarity){EA10}.
FT   ACT_SITE     72     72       Proton acceptor (By similarity){EA10}.
FT   ACT_SITE    193    193       Proton donor (By similarity){EA10}.
FT   BINDING       9      9       3-amino-2-oxopropyl phosphate (By
FT                                similarity){EA10}.
FT   BINDING      20     20       3-amino-2-oxopropyl phosphate (By
FT                                similarity){EA10}.
FT   BINDING      47     47       1-deoxy-D-xylulose 5-phosphate (By
FT                                similarity){EA10}.
FT   BINDING      52     52       1-deoxy-D-xylulose 5-phosphate (By
FT                                similarity){EA10}.
FT   BINDING     102    102       1-deoxy-D-xylulose 5-phosphate (By
FT                                similarity){EA10}.
FT   BINDING     194    194       3-amino-2-oxopropyl phosphate; via amide
FT                                nitrogen (By similarity){EA10}.
FT   SITE        153    153       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   243 AA;  26344 MW;  82E7DF71CB6BA15E CRC64;
     MADLLLGVNI DHIATLRNAR GTQYPDPVQA AFIAEQAGAD GITVHLREDR RHITDRDVRI
     LRQTIQTRMN LEMAVTDEML DIAIELKPQF CCLVPEKREE VTTEGGLDVA GQQDKMAVAV
     ERLAQAGILV SLFIDPDHRQ IDAAVAVGAP YIEIHTGAYA EATGEMAVKA ELHRIAVAAT
     YAAGKGLKVN AGHGLTYHNV QPIAALPEMY ELNIGHAIIG QAVMSGLPAA VADMKLLMRE
     ARR
//
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