ADHS_METM5
ID ADHS_METM5 Reviewed; 272 AA.
AC A4FYB3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=MmarC5_0890;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO35197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000609; ABO35197.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048058462.1; NC_009135.1.
DR AlphaFoldDB; A4FYB3; -.
DR SMR; A4FYB3; -.
DR STRING; 402880.MmarC5_0890; -.
DR EnsemblBacteria; ABO35197; ABO35197; MmarC5_0890.
DR GeneID; 4928772; -.
DR KEGG; mmq:MmarC5_0890; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_0_2; -.
DR OrthoDB; 57391at2157; -.
DR Proteomes; UP000000253; 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; Schiff base;
KW Transferase.
FT CHAIN 1..272
FT /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT synthase"
FT /id="PRO_0000363664"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 184
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT BINDING 33..37
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 153..155
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 209..210
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 237..238
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 272 AA; 29343 MW; AEDC1F1490E79FC6 CRC64;
MKMFDNIKNV GKLIRLERIF DKKSEKTVII PMDHGVSSGP LDGIKDMRIT TNAVADGGAN
AVLGHKGLVR HGHRGYGRDI GLIIHMSAGT SISPDPNKKV IVTTVEDAIR LGADAVSLHV
NVGAESDFEM YRDLGLISET CEQWGMPLIA MMYPRGPKIK DEKDPEVVAH AARLGAELGA
DIIKTNYTGD PDTFKEVVKG CPAPIVIAGG PKTNTDEEFL QMVKDAMHAG GKGVASGRNV
FQHKDVKGIT SAICKIVHED AEVKEALKEI KI
