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PDXJ_ACIAD
ID   PDXJ_ACIAD              Reviewed;         241 AA.
AC   Q3V7G6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00279};
DE            Short=PNP synthase {ECO:0000255|HAMAP-Rule:MF_00279};
DE            EC=2.6.99.2 {ECO:0000255|HAMAP-Rule:MF_00279};
GN   Name=pdxJ {ECO:0000255|HAMAP-Rule:MF_00279}; OrderedLocusNames=ACIAD2577;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00279}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00279}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00279}.
CC   -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00279}.
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DR   EMBL; CR543861; CAG69340.1; -; Genomic_DNA.
DR   RefSeq; WP_004928715.1; NC_005966.1.
DR   AlphaFoldDB; Q3V7G6; -.
DR   SMR; Q3V7G6; -.
DR   STRING; 62977.ACIAD2577; -.
DR   EnsemblBacteria; CAG69340; CAG69340; ACIAD2577.
DR   GeneID; 45234860; -.
DR   KEGG; aci:ACIAD2577; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_0_0_6; -.
DR   OMA; SNAGWDT; -.
DR   OrthoDB; 1159993at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11715-MON; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000000430; Chromosome.
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; -; 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   PANTHER; PTHR30456; PTHR30456; 1.
DR   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; SSF63892; 1.
DR   TIGRFAMs; TIGR00559; pdxJ; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pyridoxine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..241
FT                   /note="Pyridoxine 5'-phosphate synthase"
FT                   /id="PRO_0000231777"
FT   ACT_SITE        44
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         8
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         10..11
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         19
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         46
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         51
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         101
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         193
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         214..215
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   SITE            152
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   241 AA;  25994 MW;  AF487CAE41E619C2 CRC64;
     MAALLGVNID HVATLRQARG TRYPDPVSAA LVCEQAGAEG ITLHLREDRR HIQDDDVRRM
     RPLLKTRMNL ELAVTDEMIA FAKEIQPQHV CFVPERRQEV TTEGGLDVVG QFEKVKAATQ
     TLAAVGCDVS LFIDADLAQI DAAIACGAPT IELHTGAYAD AETEEQQQAE LQRIIEGVEY
     AASKGLVVNA GHGLNLDNIT PIAAIPQIHE LNIGHSIIAD SVFVGLAQAV QHMKAAIQAA
     R
 
 
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