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Database: UniProt
Entry: A0A242AWN4_9ENTE
LinkDB: A0A242AWN4_9ENTE
Original site: A0A242AWN4_9ENTE 
ID   A0A242AWN4_9ENTE        Unreviewed;       342 AA.
AC   A0A242AWN4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
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=A5821_000947 {ECO:0000313|EMBL:OTN85018.1};
OS   Enterococcus sp. 7F3_DIV0205.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834189 {ECO:0000313|EMBL:OTN85018.1, ECO:0000313|Proteomes:UP000194948};
RN   [1] {ECO:0000313|EMBL:OTN85018.1, ECO:0000313|Proteomes:UP000194948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7F3_DIV0205 {ECO:0000313|EMBL:OTN85018.1,
RC   ECO:0000313|Proteomes:UP000194948};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 7F3_DIV0205.";
RL   Submitted (MAY-2017) 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:OTN85018.1}.
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DR   EMBL; NGKX01000001; OTN85018.1; -; Genomic_DNA.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000194948; 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:UP000194948};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       34    334       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   342 AA;  38729 MW;  6D65CCCAAFA3314D CRC64;
     MSFKTLSQPI NFEQVKSLSK LTPEQEQLKA ARDQELKEII EGKSDKILLV IGPCSAHNED
     AVMEYVTRLA KLQEKVQEKI FMVPRVYTNK PRTNGDGYKG LLHQQNPEGE SNLIKGIAAV
     RSLHNRVISE TGLTTADEML YPENLEFVQD LVSYIAVGAR SVEDQQHRFV ASGIDQPTGM
     KNPTSGNLKV LFNSLYAAQQ KQEFIFNGLE VESSSNPLAH VVLRGGLNEY GENIPNYHYE
     DLLKVVELYK AGNYKNPFIV IDTNHDNSGK QYKEQIRIVK ETLINRSWNS EMKNWVRGFM
     IESFLESGRQ EADGKVFGQS ITDPCIGWDE TEQLVNYIAE HA
//
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