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Database: UniProt
Entry: G6EQH7_STRTR
LinkDB: G6EQH7_STRTR
Original site: G6EQH7_STRTR 
ID   G6EQH7_STRTR            Unreviewed;       343 AA.
AC   G6EQH7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   08-MAY-2019, entry version 31.
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=STHE1630_01374 {ECO:0000313|EMBL:EHE88570.1};
OS   Streptococcus thermophilus CNCM I-1630.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1042404 {ECO:0000313|EMBL:EHE88570.1};
RN   [1] {ECO:0000313|EMBL:EHE88570.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1630 {ECO:0000313|EMBL:EHE88570.1};
RX   PubMed=22030749;
RA   McNulty N.P., Yatsunenko T., Hsiao A., Faith J.J., Muegge B.D.,
RA   Goodman A.L., Henrissat B., Oozeer R., Cools-Portier S., Gobert G.,
RA   Chervaux C., Knights D., Lozupone C.A., Knight R., Duncan A.E.,
RA   Bain J.R., Muehlbauer M.J., Newgard C.B., Heath A.C., Gordon J.I.;
RT   "The impact of a consortium of fermented milk strains on the gut
RT   microbiome of gnotobiotic mice and monozygotic twins.";
RL   Sci. Transl. Med. 3:106RA106-106RA106(2011).
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:EHE88570.1}.
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DR   EMBL; AGFN01000346; EHE88570.1; -; Genomic_DNA.
DR   EnsemblBacteria; EHE88570; EHE88570; STHE1630_01374.
DR   PATRIC; fig|1042404.3.peg.1582; -.
DR   BioCyc; STHE1042404:G12HI-546-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
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   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:EHE88570.1}.
FT   DOMAIN       35    332       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   343 AA;  38673 MW;  41E32A0EAE6D0CF6 CRC64;
     MGIHKISSLI DTAEVRKAHA LTGDDLAKKQ VNDSALAKII KGEDDRLLLV IGPCSSDNEK
     AVLDYAHRLS KLQEEVKDKI FIVMRVYTAK PRTNGDGYKG LVHQPDSEGA TDLITGIKAV
     RRLQSRIIRE TGLPLADEML YPTNLIYFED LLSYHAIGAR SVEDQEHRFV ASGLDVPTGL
     KNPTSGNLNV MFNAIYAAHN EQEFIYNGHE VKTDGNPLAH AILRGSSNEY GQNEVNYHYE
     DLVKALDKYS EFGLENPFIL VDTNHDNSGK NFMEQIRIVR EVLLNREWDK RIADTVRGFM
     IESYLEDGRQ DTPEVYGKSI TDPCLGWEKT VNLIREIHTT LSK
//
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