ADHS2_ARCFU
ID ADHS2_ARCFU Reviewed; 265 AA.
AC O30128;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase 2;
DE Short=ADH synthase 2 {ECO:0000255|HAMAP-Rule:MF_00960};
DE Short=ADHS 2 {ECO:0000255|HAMAP-Rule:MF_00960};
DE Short=ADTH synthase 2 {ECO:0000255|HAMAP-Rule:MF_00960};
DE EC=2.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00960};
GN OrderedLocusNames=AF_0108;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(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; AE000782; AAB91123.1; -; Genomic_DNA.
DR PIR; D69263; D69263.
DR RefSeq; WP_010877622.1; NC_000917.1.
DR AlphaFoldDB; O30128; -.
DR SMR; O30128; -.
DR STRING; 224325.AF_0108; -.
DR PRIDE; O30128; -.
DR EnsemblBacteria; AAB91123; AAB91123; AF_0108.
DR GeneID; 1483320; -.
DR KEGG; afu:AF_0108; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_0_2; -.
DR OMA; CEYWGMP; -.
DR OrthoDB; 57391at2157; -.
DR PhylomeDB; O30128; -.
DR Proteomes; UP000002199; 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..265
FT /note="Putative 2-amino-3,7-dideoxy-D-threo-hept-6-
FT ulosonate synthase 2"
FT /id="PRO_0000138953"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT ACT_SITE 147
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 27..31
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 147..149
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 265 AA; 28168 MW; 2950F9D9F9A0F870 CRC64;
MTKIGKKIRI ERIINRESRN TVIVPMDHGV SMGPIEGLKN LAETVNAVAE GGANAVVLHK
GVVGFGHRGY GKDVGLIIHL SASTSLAPDP NEKVLVCTVE EAIKLGADAV SVHVNVGSKT
EAYQLRKLGE ISKIAGEWGM PLLAMMYPRG DGINQFDEKA VALAARVGAE LGADIIKTNF
TGDVESFRRV VDGCPVPVVV AGGPKMGSDE DILRMVRMAM DAGARGVAIG RNIFQANNPT
KMTRAISMIV HDNADVSEAL EFLKS
