ADHS_METTH
ID ADHS_METTH Reviewed; 266 AA.
AC O26679;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=MTH_579;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85085.1; -; Genomic_DNA.
DR PIR; F69176; F69176.
DR RefSeq; WP_010876218.1; NC_000916.1.
DR AlphaFoldDB; O26679; -.
DR SMR; O26679; -.
DR STRING; 187420.MTH_579; -.
DR EnsemblBacteria; AAB85085; AAB85085; MTH_579.
DR GeneID; 24853716; -.
DR KEGG; mth:MTH_579; -.
DR PATRIC; fig|187420.15.peg.558; -.
DR HOGENOM; CLU_057069_2_0_2; -.
DR OMA; MHVNIGA; -.
DR Proteomes; UP000005223; 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR TIGRFAMs; TIGR01949; AroFGH_arch; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..266
FT /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT synthase"
FT /id="PRO_0000138959"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 176
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 25..29
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 145..147
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 201..202
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 229..230
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 266 AA; 28013 MW; 9381A9AACA28EB2C CRC64;
MIGKRIRIER IINRKTDRTV IVPLDHGVSI GPVRGIIDMA GTIDEVASGG ANAVLMHKGM
VRSGHRGYGR DIGLIIHLSA STGLGPDPNH KVLVTSVEKA LKLGADAVSV HVNVGSEREP
EMLIKLGTVA EICDDWGMPL IAMMYPRGKK IDDEHDPEVV KLAARAGAEL GADIIKTNYT
GDPDTFRDVV KGCPVPVVIA GGPKIETEEE LLQMVSDSVE AGGAGVAIGR NIFQADSPAN
MTGAIAGIVH DGLSVEEAVR ILKGGE
