GenomeNet

Database: UniProt
Entry: D4J3X5_9FIRM
LinkDB: D4J3X5_9FIRM
Original site: D4J3X5_9FIRM 
ID   D4J3X5_9FIRM            Unreviewed;       347 AA.
AC   D4J3X5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=CC1_00680 {ECO:0000313|EMBL:CBK79046.1};
OS   Coprococcus catus GD/7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK79046.1, ECO:0000313|Proteomes:UP000008798};
RN   [1] {ECO:0000313|EMBL:CBK79046.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK79046.1,
RC   ECO:0000313|Proteomes:UP000008798};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Coprococcus catus GD/7.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK79046.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK79046.1,
RC   ECO:0000313|Proteomes:UP000008798};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {ECO:0000256|ARBA:ARBA00003726,
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; EC=2.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00001370,
CC         ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP929038; CBK79046.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4J3X5; -.
DR   STRING; 717962.CC1_00680; -.
DR   KEGG; cct:CC1_00680; -.
DR   PATRIC; fig|717962.3.peg.59; -.
DR   HOGENOM; CLU_030903_0_0_9; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000008798; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          37..338
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   347 AA;  39210 MW;  F46A82AC2B6D6841 CRC64;
     MNHEQMQMEF VRKLPIPQEI KKQFPISEKI AQHKAERDEA IRRVFTGESD KFLLIIGPCS
     ADSEEPVMEY IHRLARVQEK VADKIIMIPR IYTNKPRTTG KGYKGMLHQP DPEKQPDLLE
     GLIAIRKLHA RAIEETGLTC ADEMLYPENH RYLSDLLSYV AVGARSVEDQ IHRLTGSGVG
     IPCGMKNPMS GDISVMLNSI EAAQSPQMFV YRGWEVKTPG NPLAHAILRG AVNEHGNNIP
     NYHFENLSQL YDSYAEKGLE NMGCIIDTNH SNSSKQYMAQ IRIANEVMHS RRHSDDIKKL
     VKGFMIESYL EDGSQKIGEG VFGKSITDPC LGWEKTEALI YSIAEQL
//
DBGET integrated database retrieval system