ID A0A497XRH7_9AQUI Unreviewed; 268 AA.
AC A0A497XRH7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADH synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADHS {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADTH synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE EC=2.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00960};
GN Name=aroA' {ECO:0000256|HAMAP-Rule:MF_00960};
GN ORFNames=BCF55_1178 {ECO:0000313|EMBL:RLJ70891.1};
OS Hydrogenivirga caldilitoris.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=246264 {ECO:0000313|EMBL:RLJ70891.1, ECO:0000313|Proteomes:UP000267841};
RN [1] {ECO:0000313|EMBL:RLJ70891.1, ECO:0000313|Proteomes:UP000267841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16510 {ECO:0000313|EMBL:RLJ70891.1,
RC ECO:0000313|Proteomes:UP000267841};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00960};
CC -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_00960}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00960}.
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:RLJ70891.1}.
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DR EMBL; RCCJ01000001; RLJ70891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A497XRH7; -.
DR OrthoDB; 5915071at2; -.
DR Proteomes; UP000267841; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00960};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00960};
KW Reference proteome {ECO:0000313|Proteomes:UP000267841};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00960};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00960}.
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960,
FT ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 177
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 177
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00960"
SQ SEQUENCE 268 AA; 28580 MW; CEEC1F3942A03717 CRC64;
MNIGKVVRLE RIMNRNTRRT IIVPMDHGVS SGPIEGIKDI KVAVDKVAEG GANAVVLHKG
MVRAGHRGGG KDIGLIVHLS ASTDLSPSKN DKVLVCSVEE AIRLGADAVS IHVNIGADME
RDMLRDFGII SRACEEWQMP LLAMVYGRGP KIENQYDPKV VAHCARIGAE LGADIVKVPY
SGDPESFRLA TEGSPIPVVI AGGPKMKSER DVLEMVHGAI RAGASGLSIG RNIFQAKDPG
LMVRAMAKIV HEGGSVEEAL EILGQTQT
//
