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Database: UniProt
Entry: I3WJW7_BIFBI
LinkDB: I3WJW7_BIFBI
Original site: I3WJW7_BIFBI 
ID   I3WJW7_BIFBI            Unreviewed;       376 AA.
AC   I3WJW7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   16-OCT-2019, entry version 35.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   ORFNames=BBB_1589 {ECO:0000313|EMBL:AFL05180.1};
OS   Bifidobacterium bifidum BGN4.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL05180.1, ECO:0000313|Proteomes:UP000006173};
RN   [1] {ECO:0000313|EMBL:AFL05180.1, ECO:0000313|Proteomes:UP000006173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGN4 {ECO:0000313|EMBL:AFL05180.1,
RC   ECO:0000313|Proteomes:UP000006173};
RX   PubMed=22887663; DOI=10.1128/JB.00988-12;
RA   Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K.,
RA   Park M.S., Ji G.E., Oh T.K., Kim J.F.;
RT   "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT   bifidum Strain BGN4.";
RL   J. Bacteriol. 194:4757-4758(2012).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP)
CC       and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-
CC       arabino-heptulosonate-7-phosphate (DAHP).
CC       {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702;
CC         EC=2.5.1.54; Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 1/7. {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP001361; AFL05180.1; -; Genomic_DNA.
DR   RefSeq; WP_014760639.1; NC_017999.1.
DR   EnsemblBacteria; AFL05180; AFL05180; BBB_1589.
DR   KEGG; bbf:BBB_1589; -.
DR   PATRIC; fig|484020.3.peg.1573; -.
DR   KO; K01626; -.
DR   OrthoDB; 853329at2; -.
DR   BioCyc; BBIF484020:G1H5L-1594-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000006173; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006173};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:AFL05180.1}.
FT   DOMAIN       64    363       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   376 AA;  41037 MW;  4786E3422BEC445D CRC64;
     MAGLRGPDSS EDERHLGGNA VFPETVDVNI RQLDPIPAPR YFLRELPLTD DMSDLVLQSR
     QEIRDILHGR DDRLLVIVGP CSIHDPKAAH EYAQRLAALK GELEDRLMIV MRVYFEKPRT
     TIGWKGLIND PDLDGRFDIR KGMWLARKVL TDVLGLGLPT ATEWLDPITP QYICDLISWG
     AIGARNTESQ VHRELASGMS MPIGFKNATD GSIKPAADSC FAAGFEHHFL SINLDGRVIS
     AETKGNPDCH LILRGSNTGP NYDAASVAAA LEALRASKAS GPSERGLVID AAHGNCGKDE
     NVEAEVIENI ASRIADGEPG ILGVMMESFL KGGHQKPAPL DQLVYGQSVT DSCVPWERTE
     ELLHTLADAI DTRHAL
//
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