ID G0BHK1_9ENTR Unreviewed; 243 AA.
AC G0BHK1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 19-FEB-2014, entry version 17.
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).
FT ACT_SITE 72 72 Proton acceptor (By similarity).
FT ACT_SITE 193 193 Proton donor (By similarity).
FT BINDING 9 9 3-amino-2-oxopropyl phosphate (By
FT similarity).
FT BINDING 20 20 3-amino-2-oxopropyl phosphate (By
FT similarity).
FT BINDING 47 47 1-deoxy-D-xylulose 5-phosphate (By
FT similarity).
FT BINDING 52 52 1-deoxy-D-xylulose 5-phosphate (By
FT similarity).
FT BINDING 102 102 1-deoxy-D-xylulose 5-phosphate (By
FT similarity).
FT BINDING 194 194 3-amino-2-oxopropyl phosphate; via amide
FT nitrogen (By similarity).
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
//
