AROF_THEMA
ID AROF_THEMA Reviewed; 338 AA.
AC Q9WYH8;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
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=aroF; OrderedLocusNames=TM_0343;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=12743122; DOI=10.1074/jbc.m304631200;
RA Wu J., Howe D.L., Woodard R.W.;
RT "Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)
RT synthase: the ancestral eubacterial DAHP synthase?";
RL J. Biol. Chem. 278:27525-27531(2003).
CC -!- FUNCTION: Catalyzes the condensation of phosphoenolpyruvate (PEP) and
CC D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC heptulosonate-7-phosphate (DAHP).
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Note=Divalent metal ions.;
CC -!- ACTIVITY REGULATION: Inhibited by L-phenylalanine and L-tyrosine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.3 at 60 degrees Celsius.;
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Extremely thermostable.;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35429.1; -; Genomic_DNA.
DR PIR; E72388; E72388.
DR RefSeq; NP_228154.1; NC_000853.1.
DR RefSeq; WP_004083125.1; NZ_CP011107.1.
DR PDB; 1RZM; X-ray; 2.20 A; A/B=1-338.
DR PDB; 1VR6; X-ray; 1.92 A; A/B/C/D=1-338.
DR PDB; 3PG8; X-ray; 2.00 A; A/B=71-338.
DR PDB; 3PG9; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-338.
DR PDB; 4GRS; X-ray; 3.00 A; A/B/C/D=1-103.
DR PDBsum; 1RZM; -.
DR PDBsum; 1VR6; -.
DR PDBsum; 3PG8; -.
DR PDBsum; 3PG9; -.
DR PDBsum; 4GRS; -.
DR AlphaFoldDB; Q9WYH8; -.
DR SMR; Q9WYH8; -.
DR STRING; 243274.THEMA_03000; -.
DR DrugBank; DB03937; D-erythrose 4-phosphate.
DR DrugBank; DB01819; Phosphoenolpyruvate.
DR EnsemblBacteria; AAD35429; AAD35429; TM_0343.
DR KEGG; tma:TM0343; -.
DR eggNOG; COG2876; Bacteria.
DR InParanoid; Q9WYH8; -.
DR OMA; SMTIQEF; -.
DR OrthoDB; 687380at2; -.
DR BRENDA; 2.5.1.54; 6331.
DR UniPathway; UPA00053; UER00084.
DR EvolutionaryTrace; Q9WYH8; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR041071; DAHP_snth_FXD.
DR InterPro; IPR006268; DAHP_syn_2.
DR Pfam; PF18152; DAHP_snth_FXD; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01361; DAHP_synth_Bsub; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..338
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase"
FT /id="PRO_0000140847"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1VR6"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3PG8"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1RZM"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1VR6"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:1VR6"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1VR6"
SQ SEQUENCE 338 AA; 37378 MW; E9634B6704D3DF4D CRC64;
MIVVLKPGST EEDIRKVVKL AESYNLKCHI SKGQERTVIG IIGDDRYVVA DKFESLDCVE
SVVRVLKPYK LVSREFHPED TVIDLGDVKI GNGYFTIIAG PCSVEGREML METAHFLSEL
GVKVLRGGAY KPRTSPYSFQ GLGEKGLEYL REAADKYGMY VVTEALGEDD LPKVAEYADI
IQIGARNAQN FRLLSKAGSY NKPVLLKRGF MNTIEEFLLS AEYIANSGNT KIILCERGIR
TFEKATRNTL DISAVPIIRK ESHLPILVDP SHSGGRRDLV IPLSRAAIAV GAHGIIVEVH
PEPEKALSDG KQSLDFELFK ELVQEMKKLA DALGVKVN
