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Database: UniProt
Entry: A0A086ZTQ5_9BIFI
LinkDB: A0A086ZTQ5_9BIFI
Original site: A0A086ZTQ5_9BIFI 
ID   A0A086ZTQ5_9BIFI        Unreviewed;       376 AA.
AC   A0A086ZTQ5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-MAY-2019, entry version 23.
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=BBIA_1827 {ECO:0000313|EMBL:KFI49905.1};
OS   Bifidobacterium biavatii DSM 23969.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI49905.1, ECO:0000313|Proteomes:UP000029108};
RN   [1] {ECO:0000313|EMBL:KFI49905.1, ECO:0000313|Proteomes:UP000029108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI49905.1,
RC   ECO:0000313|Proteomes:UP000029108};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFI49905.1}.
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DR   EMBL; JGYN01000019; KFI49905.1; -; Genomic_DNA.
DR   RefSeq; WP_033494666.1; NZ_JGYN01000019.1.
DR   STRING; 1437608.BBIA_1827; -.
DR   EnsemblBacteria; KFI49905; KFI49905; BBIA_1827.
DR   OrthoDB; 853329at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000029108; Unassembled WGS sequence.
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:UP000029108};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029108};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:KFI49905.1}.
FT   DOMAIN       62    363       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   376 AA;  40913 MW;  E055681F3F384CC1 CRC64;
     MAGLRGPDSS EDERQLSKNA VFPETVDVNI RQLDPIPAPR YFLKELPLTD EMSDLVLQSR
     QQIRDILHGK DDRLLVIVGP CSIHDPKAAH EYATKLAAVA KELSDRLLIV MRVYFEKPRT
     TIGWKGLIND PDLNGRFDIR KGMWLARKVL TDVLSLGLPT ATEWLDPITP QYICDLISWG
     AIGARNTESQ VHRELASGLS MPVGFKNATD GSIKPAADSC YAAAFEHHFL SINLDGRVIS
     AETKGNPDCH LVLRGSNSGP NYDAASVAQA LADLKKSKAS GPSEHGLIID AAHGNCGKDE
     KVEAEVVENI ASRIAAGEQG ILGVMMESFL VAGHQKPAPL DQLVYGQSVT DSCVPWDRTE
     QLLHTLADAV AARRTA
//
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