ID   AROF_STRCO              Reviewed;         450 AA.
AC   P80574; Q9S2M8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 133.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=aroH; OrderedLocusNames=SCO2115; ORFNames=SC6E10.09c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-22, AND CHARACTERIZATION.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8760910; DOI=10.1099/13500872-142-8-1973;
RA   Walker G.E., Dunbar B., Hunter I.S., Nimmo H.G., Coggins J.R.;
RT   "Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-
RT   phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus
RT   and Neurospora crassa.";
RL   Microbiology 142:1973-1982(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AL939111; CAB51963.1; -; Genomic_DNA.
DR   PIR; T35496; T35496.
DR   RefSeq; WP_003976701.1; NC_003888.3.
DR   AlphaFoldDB; P80574; -.
DR   SMR; P80574; -.
DR   FunCoup; P80574; 295.
DR   STRING; 100226.gene:17759713; -.
DR   PaxDb; 100226-gene:17759713; -.
DR   GeneID; 97465488; -.
DR   KEGG; sco:SCO2115; -.
DR   PATRIC; fig|100226.15.peg.2149; -.
DR   eggNOG; COG3200; Bacteria.
DR   HOGENOM; CLU_026885_0_1_11; -.
DR   InParanoid; P80574; -.
DR   OrthoDB; 9766852at2; -.
DR   PhylomeDB; P80574; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000001973; Chromosome.
DR   AbasyAtlas; P80574; -.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
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; IPR002480; DAHP_synth_2.
DR   NCBIfam; TIGR01358; DAHP_synth_II; 1.
DR   PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR   Pfam; PF01474; DAHP_synth_2; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52062; DAHPS_II; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Direct protein sequencing; Metal-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8760910"
FT   CHAIN           2..450
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase"
FT                   /id="PRO_0000140854"
FT   DOMAIN          64..450
FT                   /note="DAHPS class-II TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         113
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         270..271
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         293
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         324
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         356
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         398
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         428
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   CONFLICT        15..22
FT                   /note="WRDLPAAQ -> DDPLQAPS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  49870 MW;  074668C290250874 CRC64;
     MTVNAKTSPS AGNTWRDLPA AQQPEYPDTE ALRAVIADLE SYPPLVFAGE CDQLRARMAA
     VAKGEAFLLQ GGDCAEAFDA VSADHIRNKL KTLLQMGAVL TYAASVPVVK VGRIAGQYSK
     PRSKPTETRD GVTLPTYRGD SVNGFDFTEA ARIPDPERLK RMYHASASTL NLVRAFTTGG
     YADLRQVHAW NQDFVKSSPS GQRYEQLARE IDNALNFMRA CGTDPAEFQT VEFFSSHEAL
     LLDYESALTR VDSRTGQLYD VSGHMVWIGE RTRQLDHAHI EFASRIRNPI GIKLGPSTTA
     EEALQYIERL DPEREPGRLT FIVRMGADKI RDKLPELVEK VTASGATVAW ITDPMHGNTY
     EAASGHKTRR FDDVLDEVKG FFEVHKSLGT HPGGIHVELT GDDVTECVGG GDEIFVDDLH
     QRYETACDPR LNRSQSLDLA FLVAEMYRDQ
//