ID A3CLD4_STRSV Unreviewed; 343 AA.
AC A3CLD4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN Name=aroG {ECO:0000313|EMBL:ABN43989.1};
GN OrderedLocusNames=SSA_0544 {ECO:0000313|EMBL:ABN43989.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43989.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43989.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43989.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN43989.1; -; Genomic_DNA.
DR RefSeq; WP_002901054.1; NC_009009.1.
DR RefSeq; YP_001034539.1; NC_009009.1.
DR AlphaFoldDB; A3CLD4; -.
DR STRING; 388919.SSA_0544; -.
DR GeneID; 61535879; -.
DR KEGG; ssa:SSA_0544; -.
DR PATRIC; fig|388919.9.peg.525; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_0_9; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000002148; 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 Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 38..333
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 343 AA; 38626 MW; 63EAF1D9D039DD22 CRC64;
MTFKATSQPI DVAEVRQLAK LEGDMLARKE KRDRELEAIL RGQDDRILLV IGPCSSDNEE
AVLEYAKRLS ALQEEVKDRI FMVMRVYTAK PRTNGDGYKG LIHQPNATAA PSLINGIKAV
RNLHYRVISE TGMTTADEML YPENLPLVDD LISYMAVGAR SVEDQQHRFV ASGADLPTGL
KNPTSGNLNV MFNGIYAAQN KQSFLFAGKE VETSGNPLAH AILRGALNEY GKNIPNYYYD
NLLDTIAQYE KMGLENPFII IDTNHDNSGK QYLEQVRIVR QTLINRDWNE KIKATVRGFM
IESYLEDGRQ DEPEVFGKSI TDPCLGWANT EQLVREIYDT LGK
//
