ID DAPA_METMP Reviewed; 289 AA. AC Q6LZP8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 114. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=MMP0576; OS Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 OS / LL). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanococcaceae; Methanococcus. OX NCBI_TaxID=267377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14266 / JCM 13030 / NBRC 101832 / 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). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4- CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H(+); CC Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00418}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase CC (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde CC [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was CC shown in E.coli that the product of the enzymatic reaction is not CC dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)- CC dipicolinic acid (HTPA), and that the consecutive dehydration reaction CC leading to DHDP is not spontaneous but catalyzed by DapB. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX950229; CAF30132.1; -; Genomic_DNA. DR RefSeq; WP_011170520.1; NC_005791.1. DR AlphaFoldDB; Q6LZP8; -. DR SMR; Q6LZP8; -. DR STRING; 267377.MMP0576; -. DR EnsemblBacteria; CAF30132; CAF30132; MMP0576. DR GeneID; 2761834; -. DR KEGG; mmp:MMP0576; -. DR PATRIC; fig|267377.15.peg.589; -. DR eggNOG; arCOG04172; Archaea. DR HOGENOM; CLU_049343_7_1_2; -. DR OrthoDB; 33636at2157; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000000590; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-ARBA. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule. DR CDD; cd00950; DHDPS; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00418; DapA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR NCBIfam; TIGR00674; dapA; 1. DR PANTHER; PTHR12128:SF66; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lyase; KW Lysine biosynthesis; Reference proteome; Schiff base. FT CHAIN 1..289 FT /note="4-hydroxy-tetrahydrodipicolinate synthase" FT /id="PRO_0000103200" FT ACT_SITE 131 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT ACT_SITE 160 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 43 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 200 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 42 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 105 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" SQ SEQUENCE 289 AA; 31584 MW; A5EAA59A4678503D CRC64; MQGVYPAIIT PLKENKVDYD GLRNNIDFLI ENGVSGVIPV GTTGESPTLT PLEHEKVVEK VVEFVDGRVE VIAGTGSNST SEALEFSQYA EDVGVDGVLL ITPYYNKPTQ EGLKRHFGEI ANSINVPIVL YNVPSRTALN IEPETIKYLF NEYSNISAVK EANPNLSQVS EVLDSCDIDI LSGNDELTLP IISLGGKGVV SVIANIAPKE FVQMVDFANA GKFDKAKEIH YKLFPLMKLM FVETNPIPIK TAMNMLGMPS GELRLPLCEM AESNKLKLQN ALNNLGLLK //