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ADHS_METMP
ID   ADHS_METMP              Reviewed;         272 AA.
AC   Q6LZE3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=MMP0686;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   FUNCTION, ROLE IN DKFP PATHWAY, GENE NAME, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=17010158; DOI=10.1111/j.1365-2958.2006.05426.x;
RA   Porat I., Sieprawska-Lupa M., Teng Q., Bohanon F.J., White R.H.,
RA   Whitman W.B.;
RT   "Biochemical and genetic characterization of an early step in a novel
RT   pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic
RT   acid in the archaeon Methanococcus maripaludis.";
RL   Mol. Microbiol. 62:1117-1131(2006).
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) (Probable). Plays a key role in
CC       an 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 and which is also a precursor for the biosynthesis
CC       of p-aminobenzoic acid (PABA) in M.maripaludis. Does not possess
CC       fructose-bisphosphate (FBP) aldolase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00960, ECO:0000269|PubMed:17010158, ECO:0000305}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene require both aromatic
CC       amino acids (AroAAs) and p-aminobenzoic acid (PABA) for growth. In the
CC       presence of PABA and AroAAs, growth of the mutant strain laggs about 30
CC       hours behind that of wild-type strain. By complementing the mutant
CC       strain with the expression of aroA', the strain grows in minimal medium
CC       with acetate only. Aryl acids do not replace the requirement of AroAAs
CC       for the growth of the deletion mutant strain.
CC       {ECO:0000269|PubMed:17010158}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00960}.
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DR   EMBL; BX950229; CAF30242.1; -; Genomic_DNA.
DR   RefSeq; WP_011170630.1; NC_005791.1.
DR   AlphaFoldDB; Q6LZE3; -.
DR   SMR; Q6LZE3; -.
DR   STRING; 267377.MMP0686; -.
DR   EnsemblBacteria; CAF30242; CAF30242; MMP0686.
DR   GeneID; 41279155; -.
DR   KEGG; mmp:MMP0686; -.
DR   PATRIC; fig|267377.15.peg.703; -.
DR   eggNOG; arCOG04044; Archaea.
DR   HOGENOM; CLU_057069_2_0_2; -.
DR   OMA; CEYWGMP; -.
DR   OrthoDB; 57391at2157; -.
DR   BioCyc; MMAR267377:MMP_RS03595-MON; -.
DR   Proteomes; UP000000590; 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..272
FT                   /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT                   synthase"
FT                   /id="PRO_0000363669"
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;  29418 MW;  5102BCB8D68514EC CRC64;
     MEMFDNIKNV GKLIRLERIF DKKSEKTVII PMDHGVSSGP LDGIKDMRIT TNAVADGGAN
     AVLGHKGLVR HGHRGYGRDI GLIIHMSAGT SISPDPNKKV IVTTVEDAMR MGADAVSLHV
     NVGAESDFEM YRDLGLISET CEHWGMPLIA MMYPRGPKIK DEKDPEVVAH AARLGAELGA
     DIIKTNYTGD PDTFKEVVKG CPAPIVIAGG PKTNTDEEFL QMVKDAMHAG GKGVASGRNV
     FQHKDVKGIT SAICKIVHED VEVEEALKEI KI
 
 
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