ID DAPA_CLOPS Reviewed; 291 AA. AC Q0SRS5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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=CPR_1872; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM101 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D., RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J., RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B., RA Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen, RT Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). 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 + H(+) + H2O; 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; CP000312; ABG86666.1; -; Genomic_DNA. DR AlphaFoldDB; Q0SRS5; -. DR SMR; Q0SRS5; -. DR KEGG; cpr:CPR_1872; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000001824; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. 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:SF72; 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; Schiff base. FT CHAIN 1..291 FT /note="4-hydroxy-tetrahydrodipicolinate synthase" FT /id="PRO_1000050180" FT ACT_SITE 132 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 44 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 202 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 43 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 106 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" SQ SEQUENCE 291 AA; 31897 MW; C944090AA251C912 CRC64; MFKGSCVALI TPFTEDGVNY EELRKLLEWH IKNHTDAILV CGTTGEGSTM TLEEKKEVIK FSVEVVNKRV PVIAGTGTNN TKASIELSKY AEEVGADMVL IITPYYNKTS QKGLYAHFSA INDAINIPIM LYNVPSRTGM NITPLMLDKL ANLNNVVAIK EASGDLSQVA KMAELCGDRI AIYSGNDDQI VPILSLGGAG VVSVLANILP EETHNICEKY FLGEVIESRN LQLKYLSLAN SLFIETNPIP VKTAMNLMNF NCGPLRLPLC EMEDSNLVIL EENLKANGLI K //