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
