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Pyridoxine 5'-phosphate synthase (PNP synthase) (EC 2.6.99.2)

 A0A166AQI7_9RHOB        Unreviewed;       249 AA.
A0A166AQI7;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
25-APR-2018, entry version 11.
RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958133};
Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279};
EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958138};
Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000313|EMBL:KZL21426.1};
ORFNames=PsAD2_00720 {ECO:0000313|EMBL:KZL21426.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL21426.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL21426.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL21426.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- FUNCTION: Catalyzes the complicated ring closure reaction between
the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and
3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP)
to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958136}.
-!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-
oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2
H(2)O. {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958139}.
-!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
phosphate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958122}.
-!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
Rule:MF_00279, ECO:0000256|SAAS:SAAS00958137}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958140}.
-!- SIMILARITY: Belongs to the PNP synthase family.
{ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000256|SAAS:SAAS00958135}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00279}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL21426.1}.
-----------------------------------------------------------------------
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EMBL; LMCB01000004; KZL21426.1; -; Genomic_DNA.
RefSeq; WP_068002284.1; NZ_LMCB01000004.1.
EnsemblBacteria; KZL21426; KZL21426; PsAD2_00720.
PATRIC; fig|989403.3.peg.764; -.
UniPathway; UPA00244; UER00313.
Proteomes; UP000076577; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:UniProtKB-EC.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00003; PNPsynthase; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00279; PdxJ; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR004569; PyrdxlP_synth_PdxJ.
InterPro; IPR036130; Pyridoxine-5'_phos_synth.
PANTHER; PTHR30456; PTHR30456; 1.
Pfam; PF03740; PdxJ; 1.
SUPFAM; SSF63892; SSF63892; 1.
TIGRFAMs; TIGR00559; pdxJ; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000076577};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958134};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958120};
Reference proteome {ECO:0000313|Proteomes:UP000076577};
Transferase {ECO:0000256|HAMAP-Rule:MF_00279,
ECO:0000256|SAAS:SAAS00958119, ECO:0000313|EMBL:KZL21426.1}.
REGION 223 224 3-amino-2-oxopropyl phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00279}.
COILED 169 189 {ECO:0000256|SAM:Coils}.
ACT_SITE 46 46 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00279}.
ACT_SITE 78 78 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00279}.
ACT_SITE 200 200 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00279}.
BINDING 10 10 3-amino-2-oxopropyl phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279}.
BINDING 21 21 3-amino-2-oxopropyl phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279}.
BINDING 48 48 1-deoxy-D-xylulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279}.
BINDING 53 53 1-deoxy-D-xylulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279}.
BINDING 108 108 1-deoxy-D-xylulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00279}.
BINDING 201 201 3-amino-2-oxopropyl phosphate; via amide
nitrogen. {ECO:0000256|HAMAP-
Rule:MF_00279}.
SITE 159 159 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_00279}.
SEQUENCE 249 AA; 27526 MW; 8C8A505D0C01C85C CRC64;
MKTPSRLSVN VNAVAVLRNR RDLPWPSVTH LSALALNAGA KGITIHPRPD ERHIRHSDVL
DLSQMLKTEQ QGKELCLEGY PDQRFMDLIE KVRPTQVLFV PDDPSQQTSD HGWDFAAHMD
LLKEVIAKAK SWDIRTSLFV DPDPTQPALA AEAGAERIEI YTGPYGACYS DKEAEKHELE
KVVATAQAAK AAGLLVNAGH DLTVENLPAL IERVPYISEV SIGHGFTADA LIYGFAESVR
RFRKALAEI


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