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Database: UniProt
Entry: F7SV12_9BURK
LinkDB: F7SV12_9BURK
Original site: F7SV12_9BURK 
ID   F7SV12_9BURK            Unreviewed;       246 AA.
AC   F7SV12;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE            Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279};
DE            EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279};
GN   Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279};
GN   ORFNames=AXXA_02512 {ECO:0000313|EMBL:EGP48098.1};
OS   Achromobacter insuavis AXX-A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP48098.1, ECO:0000313|Proteomes:UP000004853};
RN   [1] {ECO:0000313|EMBL:EGP48098.1, ECO:0000313|Proteomes:UP000004853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AXX-A {ECO:0000313|EMBL:EGP48098.1,
RC   ECO:0000313|Proteomes:UP000004853};
RA   Bador J., Amoureux L., Neuwirth C.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the complicated ring closure reaction between the
CC       two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-
CC       2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form
CC       pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate
CC         = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate;
CC         Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58589; EC=2.6.99.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00279};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
CC       {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00279}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279}.
CC   -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00279}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGP48098.1}.
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DR   EMBL; AFRQ01000020; EGP48098.1; -; Genomic_DNA.
DR   RefSeq; WP_006390555.1; NZ_GL982453.1.
DR   AlphaFoldDB; F7SV12; -.
DR   PATRIC; fig|1003200.3.peg.481; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_0_0_4; -.
DR   OrthoDB; 9806590at2; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000004853; Unassembled WGS sequence.
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-UniRule.
DR   CDD; cd00003; PNPsynthase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00279; PdxJ; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004569; PyrdxlP_synth_PdxJ.
DR   InterPro; IPR036130; Pyridoxine-5'_phos_synth.
DR   NCBIfam; TIGR00559; pdxJ; 1.
DR   PANTHER; PTHR30456; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR30456:SF0; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; Pyridoxine 5'-phosphate synthase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00279};
KW   Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW   Rule:MF_00279}; Transferase {ECO:0000256|HAMAP-Rule:MF_00279}.
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         7
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         9..10
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         18
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         45
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         50
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         100
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         191
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         212..213
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   SITE            151
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   246 AA;  26281 MW;  E5E405D9F77558CC CRC64;
     MIELGVNIDH VATLRQQRHT AYPDPVAAAL RAEDAGADLI TLHLREDRRH IQDADVYAIR
     PQLRTRMNLE CAVTPEMLEI ACAVKPNDVC LVPEKRTELT TEGGLEVAGA LSAVSDAVGL
     LAEAGIRVSL FIDPDPAQIA AAARAGAPVI ELHTGAYAEA EGEAALAELE RIRVAVAEGL
     RHGLRVNAGH GLHYGNVKPV AALDGISELN IGHAIVAQAV FDGWEKAVRD MKALMVQARL
     EALRGR
//
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