ID ADHS_AQUAE Reviewed; 264 AA.
AC O67506;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE Short=ADH synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE Short=ADHS {ECO:0000255|HAMAP-Rule:MF_00960};
DE Short=ADTH synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE EC=2.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00960};
GN Name=aroA' {ECO:0000255|HAMAP-Rule:MF_00960}; OrderedLocusNames=aq_1554;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5-
CC ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with
CC an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-
CC dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an
CC alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ),
CC which is involved in the canonical pathway for the biosynthesis of
CC aromatic amino acids. {ECO:0000255|HAMAP-Rule:MF_00960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-
CC semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-
CC lyxo-hept-6-ulosonate; Xref=Rhea:RHEA:25952, ChEBI:CHEBI:58859,
CC ChEBI:CHEBI:58860, ChEBI:CHEBI:58861, ChEBI:CHEBI:537519;
CC EC=2.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00960};
CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00960}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00960}.
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DR EMBL; AE000657; AAC07474.1; -; Genomic_DNA.
DR PIR; H70434; H70434.
DR RefSeq; NP_214071.1; NC_000918.1.
DR RefSeq; WP_010881009.1; NC_000918.1.
DR AlphaFoldDB; O67506; -.
DR SMR; O67506; -.
DR STRING; 224324.aq_1554; -.
DR EnsemblBacteria; AAC07474; AAC07474; aq_1554.
DR KEGG; aae:aq_1554; -.
DR PATRIC; fig|224324.8.peg.1205; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_2_0_0; -.
DR InParanoid; O67506; -.
DR OrthoDB; 5915071at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00960; ADH_synthase; 1.
DR InterPro; IPR010210; ADH_synthase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR NCBIfam; TIGR01949; ADH_synth; 1.
DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..264
FT /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT synthase"
FT /id="PRO_0000138944"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 177
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 26..30
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 146..148
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 202..203
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 230..231
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
SQ SEQUENCE 264 AA; 28493 MW; 408DFD163E9CAB91 CRC64;
MGIGKEIRLE RIMNRETRKT IIVPMDHGVS SGPIEGIVNI REAVEKVAEG GANAVVLHKG
MVRAGHRGRG RDIGLIVHLS ASTDLSPRKN DKVLVCTVEE AIRLGADAVS IHVNIGAEGE
REMLKDFGYV SKVCEEWQMP LLAMVYGRGP KIENQYDPKV VAHCARVGAE LGADIVKVPY
TGDPETFKLA IEGSPIPVVI AGGPKMKSER EVLEMVQGAM QAGAAGLSIG RNIFQAKDPA
KMVRAMSLIV HEGKSVEEAF EILK
//
