ID DAPA_CHLTR Reviewed; 286 AA. AC O84366; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 04-NOV-2026, entry version 138. 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}; OrderedLocusNames=CT_361; OS Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx). OC Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales; OC Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-885 / DSM 19411 / UW-3/Cx; RX PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia RT trachomatis."; RL Science 282:754-759(1998). 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; AE001273; AAC67957.1; -; Genomic_DNA. DR PIR; F71524; F71524. DR RefSeq; NP_219870.1; NC_000117.1. DR RefSeq; WP_009871714.1; NC_000117.1. DR AlphaFoldDB; O84366; -. DR SMR; O84366; -. DR FunCoup; O84366; 146. DR STRING; 272561.CT_361; -. DR EnsemblBacteria; AAC67957; AAC67957; CT_361. DR GeneID; 884755; -. DR KEGG; ctr:CT_361; -. DR PATRIC; fig|272561.5.peg.390; -. DR HOGENOM; CLU_049343_7_0_0; -. DR InParanoid; O84366; -. DR OMA; AACFRGD; -. DR OrthoDB; 9782828at2; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central. DR GO; GO:0009085; P:L-lysine biosynthetic process; IEA:InterPro. DR CDD; cd00408; DHDPS-like; 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..286 FT /note="4-hydroxy-tetrahydrodipicolinate synthase" FT /id="PRO_0000103102" FT ACT_SITE 129 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT ACT_SITE 157 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 42 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 196 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 41 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 103 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" SQ SEQUENCE 286 AA; 31291 MW; 8CB9A156EAFDCE40 CRC64; MSVLGACITP FKADLSIDFA ALESVVRSQE HAGNGIILFG STGEGLSLTY EEKLSILSFV STLNLNVPIF VGVTATSVQE TMSWIDFAQQ WPIDGFLVPT PLYTRPGLNG QKAWFDRILS VSRKPIILYN NPIRTGVSLY PEVVKSFVSH PLCIGVKDSG GSAQACELFA ESGLRVFCGD DNLWPDMRLS GASGVISVLA NVWPELARDY VAQGRPIEAW KKVCSWLNLS TNPLGIKALM AAQKMIECDA VRPPLSIRDL QRRDELADIL ACRATLQTEL LSVCRQ //