ID PDXJ_THEEB Reviewed; 238 AA. AC Q8DKM1; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 10-AUG-2010, entry version 44. DE RecName: Full=Pyridoxine 5'-phosphate synthase; DE Short=PNP synthase; DE EC=2.6.99.2; GN Name=pdxJ; OrderedLocusNames=tlr0838; OS Thermosynechococcus elongatus (strain BP-1). OC Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus. OX NCBI_TaxID=197221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22225144; PubMed=12240834; DOI=10.1093/dnares/9.4.123; RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., RA Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the thermophilic cyanobacterium RT Thermosynechococcus elongatus BP-1."; RL DNA Res. 9:123-130(2002). 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. 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; BA000039; BAC08390.1; -; Genomic_DNA. DR RefSeq; NP_681628.1; -. DR ProteinModelPortal; Q8DKM1; -. DR SMR; Q8DKM1; 4-236. DR STRING; Q8DKM1; -. DR GeneID; 1011556; -. DR GenomeReviews; BA000039_GR; tlr0838. DR KEGG; tel:tlr0838; -. DR NMPDR; fig|197221.1.peg.837; -. DR eggNOG; COG0854; -. DR HOGENOM; HBG299314; -. DR OMA; AGHGLNY; -. DR ProtClustDB; PRK05265; -. DR BioCyc; TELO197221:TLR0838-MONOMER; -. DR BRENDA; 2.6.99.2; 277225. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:EC. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00279; PdxJ; 1; -. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004569; PyrdxlP_synth_PdxJ. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF03740; PdxJ; 1. DR SUPFAM; SSF63892; PyrdxlP_synth_PdxJ; 1. DR TIGRFAMs; TIGR00559; pdxJ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Pyridoxine biosynthesis; Transferase. FT CHAIN 1 238 Pyridoxine 5'-phosphate synthase. FT /FTId=PRO_0000190132. FT REGION 9 10 1-deoxy-D-xylulose 5-phosphate binding FT (By similarity). FT REGION 213 214 3-amino-2-oxopropyl phosphate binding (By FT similarity). FT ACT_SITE 43 43 Proton acceptor (By similarity). FT ACT_SITE 70 70 Proton acceptor (By similarity). FT ACT_SITE 191 191 Proton donor (By similarity). FT BINDING 7 7 3-amino-2-oxopropyl phosphate (By FT similarity). FT BINDING 18 18 3-amino-2-oxopropyl phosphate (By FT similarity). FT BINDING 45 45 1-deoxy-D-xylulose 5-phosphate (By FT similarity). FT BINDING 50 50 1-deoxy-D-xylulose 5-phosphate (By FT similarity). FT BINDING 100 100 1-deoxy-D-xylulose 5-phosphate (By FT similarity). FT BINDING 192 192 3-amino-2-oxopropyl phosphate; via amide FT nitrogen (By similarity). FT SITE 151 151 Transition state stabilizer (By FT similarity). SQ SEQUENCE 238 AA; 25658 MW; 6B5C6061C59D65DD CRC64; MATLGVNIDH VATIRQARRT VEPDPVAAAL LAELGGADGI TVHLREDRRH IQERDVRLLR QTVRTHLNLE MAATPEMVAI ALDIRPDYVT LVPERREEVT TEGGLDVVSQ QEPLTQVVQT LQGAGIPVSL FIDADPTQLA AAAKTTAQFI ELHTGRYAEA KGEVAQQREL AILADGVQQA KALGLRVNAG HGLTYSNVGA IARLEGIEEL NIGHTIISRA VLVGMVQAVR DMKALISP //