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Database: UniProt
Entry: S1NMH4_9ENTE
LinkDB: S1NMH4_9ENTE
Original site: S1NMH4_9ENTE 
ID   S1NMH4_9ENTE            Unreviewed;       343 AA.
AC   S1NMH4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=OMK_01649 {ECO:0000313|EMBL:EOT41473.1};
OS   Enterococcus dispar ATCC 51266.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT41473.1, ECO:0000313|Proteomes:UP000014127};
RN   [1] {ECO:0000313|EMBL:EOT41473.1, ECO:0000313|Proteomes:UP000014127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT41473.1,
RC   ECO:0000313|Proteomes:UP000014127};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT   assembly).";
RL   Submitted (MAR-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOT41473.1}.
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DR   EMBL; AHYR01000005; EOT41473.1; -; Genomic_DNA.
DR   RefSeq; WP_016172815.1; NZ_KE136354.1.
DR   AlphaFoldDB; S1NMH4; -.
DR   STRING; 44009.RV01_GL001021; -.
DR   PATRIC; fig|1139219.3.peg.1608; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_0_9; -.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000014127; 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:UP000014127};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          36..335
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   343 AA;  38713 MW;  5B3F33AB68C9D51B CRC64;
     MKMFKAISKK INAESVKSLA KLSEAEAAQK KARDLELEKI ITGEDERILL IIGPCSAHEE
     EAVMEYARRL AKLQAEVGDK VFMVPRIYTN KPRTNGDGYK GLLHQQNPNG ESNLVRGIVS
     VRKLHKRVLT ETGLTTADEM LYPENLEFVE DLVSYIAVGA RSVEDQQHRF VASGIDQPTG
     MKNPTSGNLT VLFNSLYAAQ QKQEFIYNGA EVESSSNPLA HVVLRGGLNE VGKNIPNYHY
     EDLLEVTSRY EEGNFKNPFV VVDTNHDNSG KKYLEQVRIV KETLENRNYN EKIKKMVRGF
     MIESFIEDGR QEPDGTVFGK SITDPCLGWE KTEELVRYIA EHA
//
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