ID E6IYE5_STRAP Unreviewed; 346 AA.
AC E6IYE5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=HMPREF0813_00007 {ECO:0000313|EMBL:EFU23286.1};
OS Streptococcus anginosus F0211.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=706437 {ECO:0000313|EMBL:EFU23286.1, ECO:0000313|Proteomes:UP000002973};
RN [1] {ECO:0000313|EMBL:EFU23286.1, ECO:0000313|Proteomes:UP000002973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0211 {ECO:0000313|EMBL:EFU23286.1,
RC ECO:0000313|Proteomes:UP000002973};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-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 -!- 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:EFU23286.1}.
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DR EMBL; AECT01000001; EFU23286.1; -; Genomic_DNA.
DR RefSeq; WP_003027395.1; NZ_AECT01000001.1.
DR AlphaFoldDB; E6IYE5; -.
DR eggNOG; COG0722; Bacteria.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000002973; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 34..333
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 346 AA; 39423 MW; 3857EA61F7B61228 CRC64;
MTFIEKGQKI DIDRIKETTR LSEAALIIKE KRDKELAAIL RGKDDRLLLV IGPCSSDNED
AVLEYARRLS DLQKKVADKL FMVMRVYTAK PRTNGDGYKG LVHQPNVKAA PSLINGLKAV
RNLHYRVITE TGLTTADEML YPSNLILVDD LVSYHAVGAR SVEDQEHRFV ASGLDAPIGM
KNPTSGNMNV LFNAIYVAQN KQTFLYHGQE VETSGNSLAH AILRGSINEY GKNIPNFYYE
NLLNDIQQYE EMGLEYPFIM IDTNHDNSGK RYLEQIRIVR QTLINRDWND KIKKVVRGFM
IESYLEDGRQ NEPEVFGKSI TDPCLGWDNT VRLVKEIYTT LSKNEK
//
