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Database: UniProt
Entry: A0A1I2DHC1_9FIRM
LinkDB: A0A1I2DHC1_9FIRM
Original site: A0A1I2DHC1_9FIRM 
ID   A0A1I2DHC1_9FIRM        Unreviewed;       344 AA.
AC   A0A1I2DHC1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05216245_12027 {ECO:0000313|EMBL:SFE79914.1};
OS   Succiniclasticum ruminis DSM 9236.
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Succiniclasticum.
OX   NCBI_TaxID=1123323 {ECO:0000313|EMBL:SFE79914.1, ECO:0000313|Proteomes:UP000198896};
RN   [1] {ECO:0000313|EMBL:SFE79914.1, ECO:0000313|Proteomes:UP000198896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9236 {ECO:0000313|EMBL:SFE79914.1,
RC   ECO:0000313|Proteomes:UP000198896};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FONL01000020; SFE79914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2DHC1; -.
DR   STRING; 1123323.SAMN05216245_12027; -.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000198896; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000198896};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          37..335
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   344 AA;  38426 MW;  00F5905FCCF207E4 CRC64;
     MEMQMEFIRK LPSPQELMQD YPLGAEASAA KTARDKEIRD IISGKDDRFI LVIGPCSADN
     EDAVLDYIHR LAGVQEKVKD KLMLIPRVYT NKPRTIGVGY KGMLHQANPE GKEDMLAGIT
     AIRKMHVRVV QETGLTSAEE ILYPENHRYL SDILSYAAIG ARSVEDQLHR MIASGVGIPV
     GMKNPTGGDI GVMMNSIEAA QHEQSFLFHG WEVRTKGNPL AHAILRGYVD KFGNNMPNYH
     YEDLQGLLDA YHERDVVNPA VIVDANHSNS GKKYLEQIRI SKDVMHSRQV SPDIRQLVKG
     IMIESYLEDG NQKIGGGVYG RSITDPCLGW AKSERLILEL AEMV
//
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