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Database: UniProt
Entry: J1SIE1_9STRE
LinkDB: J1SIE1_9STRE
Original site: J1SIE1_9STRE 
ID   J1SIE1_9STRE            Unreviewed;       343 AA.
AC   J1SIE1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   08-MAY-2019, entry version 33.
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=SPAR10_0263 {ECO:0000313|EMBL:EJG89400.1};
OS   Streptococcus infantis SPAR10.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1159208 {ECO:0000313|EMBL:EJG89400.1, ECO:0000313|Proteomes:UP000010312};
RN   [1] {ECO:0000313|EMBL:EJG89400.1, ECO:0000313|Proteomes:UP000010312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPAR10 {ECO:0000313|EMBL:EJG89400.1,
RC   ECO:0000313|Proteomes:UP000010312};
RA   Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E.,
RA   Pallavajjal A., Abolude O., Daugherty S.C., Parankush S.P.,
RA   Sadzewicz L., Tallon L.J., Farley M.M., Baughman W., McGee L.,
RA   Stephens D.S., Tettelin H.;
RT   "Genomic Sequence of Streptococcus mitis SPAR10.";
RL   Submitted (MAY-2012) 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:EJG89400.1}.
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DR   EMBL; ALCH01000001; EJG89400.1; -; Genomic_DNA.
DR   RefSeq; WP_004250795.1; NZ_ALCH01000001.1.
DR   EnsemblBacteria; EJG89400; EJG89400; SPAR10_0263.
DR   GeneID; 29747327; -.
DR   PATRIC; fig|1159208.3.peg.255; -.
DR   BioCyc; SMIT1159208:G129M-975-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000010312; 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:UP000010312};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:EJG89400.1}.
FT   DOMAIN       37    333       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   343 AA;  39068 MW;  6512FECA453A595B CRC64;
     MVFTAKSPKI NIDEVRSLSK LEGQVLANKL QRDQELEAII RGEDQRILLV IGPCSSDNEE
     AVLEYAKRLS KLQEEVKDRV FMVMRVYTAK PRTNGDGYKG LIHQPNAKEA PSLINGIKAV
     RHLHYRVISE TGMTTADEML YPENLPLVDD LISYMAVGAR SVEDQQHRFV ASGADFATGF
     KNPTSGNLNV MFNGIYAAQN KQSFLFLGKE VETTGNPLSH AILRGALNEY GKNIPNYYYD
     NLMDTIAQYE KMGLENPFII IDTNHDNSGK QYMEQIRIVR QTLINRDWNE KIKKYVRGFM
     IESYLEDGRQ NEPEVFGKSI TDPCLGWENT EALVREIYQR LGE
//
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