ID F0SDL3_PSESL Unreviewed; 292 AA. AC F0SDL3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000256|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=Pedsa_0154 {ECO:0000313|EMBL:ADY50740.1}; OS Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG OS 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans). OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pseudopedobacter. OX NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY50740.1, ECO:0000313|Proteomes:UP000000310}; RN [1] {ECO:0000313|EMBL:ADY50740.1, ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; RX PubMed=22180808; DOI=10.4056/sigs.2154937; RA Liolios K., Sikorski J., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Huntemann M., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., RA Kotsyurbenko O., Rohde M., Tindall B.J., Abt B., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of the gliding, heparinolytic Pedobacter saltans RT type strain (113)."; RL Stand. Genomic Sci. 5:30-40(2011). RN [2] {ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Pedobacter saltans DSM 12145."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). CC {ECO:0000256|ARBA:ARBA00003294, ECO:0000256|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:0000256|ARBA:ARBA00000594, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00005120, ECO:0000256|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_00418}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|HAMAP- CC Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365}. 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:0000256|HAMAP-Rule:MF_00418}. 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; CP002545; ADY50740.1; -; Genomic_DNA. DR RefSeq; WP_013631243.1; NC_015177.1. DR AlphaFoldDB; F0SDL3; -. DR STRING; 762903.Pedsa_0154; -. DR KEGG; psn:Pedsa_0154; -. DR eggNOG; COG0329; Bacteria. DR HOGENOM; CLU_049343_7_0_10; -. DR OrthoDB; 9782828at2; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000000310; 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 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00418}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00418}; KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_00418}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00418}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_00418}; Reference proteome {ECO:0000313|Proteomes:UP000000310}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00418}. FT ACT_SITE 135 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT ACT_SITE 164 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT BINDING 47 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-2" FT BINDING 206 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-2" FT SITE 46 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 109 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" SQ SEQUENCE 292 AA; 31574 MW; 871A8139E06C7B61 CRC64; MSRFLGTGVA MVTPFQANGS IDFDGLAATI EHLINGKVEY IVVLGTTAES ATLSKDEKKQ VFKFVTERVN GRIPLVAGIG GNNTTEVVAE VNQFEMVGYE AILSVVPYYN KPTQEGIYQH YKSIAQAAKL PIILYNVPGR TGVSMSAETT IRLAREFKNI IATKEASGSF DQFNAIMADK PEGFELISGD DPITLPMVAL GAIGVISVVG NAFPVKFSEM VRLSLNGDFK AARPLHSSFL EFTRLCFVES NPCGVKAAMK ELGIIEDYVR LPLTPIGDST RAKVVAEVAK LK //