ID A0A0E3WRM1_9EURY Unreviewed; 265 AA.
AC A0A0E3WRM1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=MSLAZ_0044 {ECO:0000313|EMBL:AKB73305.1};
OS Methanosarcina lacustris Z-7289.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB73305.1, ECO:0000313|Proteomes:UP000033072};
RN [1] {ECO:0000313|EMBL:AKB73305.1, ECO:0000313|Proteomes:UP000033072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-7289 {ECO:0000313|EMBL:AKB73305.1,
RC ECO:0000313|Proteomes:UP000033072};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00960}.
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DR EMBL; CP009515; AKB73305.1; -; Genomic_DNA.
DR RefSeq; WP_048124009.1; NZ_CP009515.1.
DR AlphaFoldDB; A0A0E3WRM1; -.
DR STRING; 1434111.MSLAZ_0044; -.
DR GeneID; 24804709; -.
DR KEGG; mls:MSLAZ_0044; -.
DR PATRIC; fig|1434111.4.peg.52; -.
DR HOGENOM; CLU_057069_2_0_2; -.
DR OrthoDB; 50091at2157; -.
DR Proteomes; UP000033072; 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 {ECO:0000256|HAMAP-Rule:MF_00960};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00960};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00960};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00960, ECO:0000313|EMBL:AKB73305.1}.
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960,
FT ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT BINDING 147..149
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 203..204
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 231..232
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 265 AA; 28680 MW; 9E477BFF19ED0832 CRC64;
MSEIGKKIRI ERLMNRESRN MVIIPMDHGL SDGPIEGLIN ITDTVNRVAE GGANAVLMQK
GMVRYGHRGY GHDIGLVVHI SASSVLSPDP NAKVQVCTVE EVLKMGADAV SMHINIGSDT
ETDQLEKLGT ISRDCTEWGM PLLAMMYPRG KKITNPHDPV NVAHAARIGA ELGADVVKTV
YTGDPDSFRD VVRGCPVPVV IAGGPKTSTD LGLLEMIDGA MEAGARGAAI GRNVFQHRDP
VRLTRAICEI VHHRRPVEEA LEQLK
//
