ADHS_METJA
ID ADHS_METJA Reviewed; 273 AA.
AC Q57843;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
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};
DE AltName: Full=Transaldolase-like ADHS;
GN Name=aroA' {ECO:0000255|HAMAP-Rule:MF_00960}; OrderedLocusNames=MJ0400;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS AN ADH SYNTHASE.
RX PubMed=15182204; DOI=10.1021/bi0495127;
RA White R.H.;
RT "L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the
RT precursors to the aromatic amino acids in Methanocaldococcus jannaschii.";
RL Biochemistry 43:7618-7627(2004).
RN [3]
RP FUNCTION AS A FBP ALDOLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=18318840; DOI=10.1111/j.1574-6968.2008.01079.x;
RA Samland A.K., Wang M., Sprenger G.A.;
RT "MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-
RT bisphosphate aldolase activity.";
RL FEMS Microbiol. Lett. 281:36-41(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP REACTION MECHANISM, SUBUNIT, AND ACTIVE SITE.
RX PubMed=17713928; DOI=10.1021/bi700934v;
RA Morar M., White R.H., Ealick S.E.;
RT "Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a
RT catalyst in the archaeal pathway for the biosynthesis of aromatic amino
RT acids.";
RL Biochemistry 46:10562-10571(2007).
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. Can also catalyze the cleavage of fructose-1,6-
CC bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and
CC dihydroxyacetone phosphate (DHAP). {ECO:0000255|HAMAP-Rule:MF_00960,
CC ECO:0000269|PubMed:15182204, ECO:0000269|PubMed:18318840}.
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 ECO:0000269|PubMed:18318840};
CC -!- ACTIVITY REGULATION: Inhibited by NaBH4 in the presence of FBP.
CC {ECO:0000269|PubMed:18318840}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=430 uM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees
CC Celsius) {ECO:0000269|PubMed:18318840};
CC Vmax=33 nmol/min/mg enzyme for the FBP aldolase activity (at pH 7 and
CC 50 degrees Celsius) {ECO:0000269|PubMed:18318840};
CC Temperature dependence:
CC Optimum temperature is not reached at 100 degrees Celsius.
CC {ECO:0000269|PubMed:18318840};
CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00960,
CC ECO:0000269|PubMed:17713928}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00960}.
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DR EMBL; L77117; AAB98389.1; -; Genomic_DNA.
DR PIR; H64349; H64349.
DR RefSeq; WP_010869899.1; NC_000909.1.
DR PDB; 2QJG; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273.
DR PDB; 2QJH; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273.
DR PDB; 2QJI; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273.
DR PDBsum; 2QJG; -.
DR PDBsum; 2QJH; -.
DR PDBsum; 2QJI; -.
DR AlphaFoldDB; Q57843; -.
DR SMR; Q57843; -.
DR STRING; 243232.MJ_0400; -.
DR EnsemblBacteria; AAB98389; AAB98389; MJ_0400.
DR GeneID; 1451260; -.
DR KEGG; mja:MJ_0400; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_0_2; -.
DR InParanoid; Q57843; -.
DR OMA; CEYWGMP; -.
DR OrthoDB; 57391at2157; -.
DR PhylomeDB; Q57843; -.
DR BioCyc; MetaCyc:MON-14592; -.
DR BRENDA; 2.2.1.10; 3260.
DR SABIO-RK; Q57843; -.
DR EvolutionaryTrace; Q57843; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..273
FT /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT synthase"
FT /id="PRO_0000138957"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:17713928"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:17713928"
FT ACT_SITE 184
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000305|PubMed:17713928"
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:0000305|PubMed:17713928"
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:0000305|PubMed:17713928"
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:0000305|PubMed:17713928"
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:0000305|PubMed:17713928"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:2QJG"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2QJG"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:2QJG"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:2QJG"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:2QJG"
SQ SEQUENCE 273 AA; 29675 MW; 06DDA2E51E8275E6 CRC64;
MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT VNDVAEGGAN
AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV IVTTVEEAIR MGADAVSIHV
NVGSDEDWEA YRDLGMIAET CEYWGMPLIA MMYPRGKHIQ NERDPELVAH AARLGAELGA
DIVKTSYTGD IDSFRDVVKG CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI
FQHDDVVGIT RAVCKIVHEN ADVEEALKEI RKK
