ID B0RGX9_CLASE Unreviewed; 327 AA. AC B0RGX9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 123. 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=CMS1198 {ECO:0000313|EMBL:CAQ01313.1}; OS Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Microbacteriaceae; Clavibacter. OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01313.1, ECO:0000313|Proteomes:UP000001318}; RN [1] {ECO:0000313|EMBL:CAQ01313.1, ECO:0000313|Proteomes:UP000001318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1 RC {ECO:0000313|Proteomes:UP000001318}; RX PubMed=18192393; DOI=10.1128/JB.01598-07; RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., RA Parkhill J., Ishimaru C.A.; RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. RT sepedonicus suggests recent niche adaptation."; RL J. Bacteriol. 190:2150-2160(2008). 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 + 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:0000256|ARBA:ARBA00047836, 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|ARBA:ARBA00007592, CC ECO:0000256|HAMAP-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; AM849034; CAQ01313.1; -; Genomic_DNA. DR RefSeq; WP_012298592.1; NC_010407.1. DR AlphaFoldDB; B0RGX9; -. DR STRING; 31964.CMS1198; -. DR GeneID; 29469936; -. DR KEGG; cms:CMS1198; -. DR eggNOG; COG0329; Bacteria. DR HOGENOM; CLU_049343_7_1_11; -. DR OrthoDB; 9782828at2; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000001318; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 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; PS00666; DHDPS_2; 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:UP000001318}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00418}. FT ACT_SITE 141 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT ACT_SITE 169 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT BINDING 53 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT BINDING 209 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 52 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 115 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" SQ SEQUENCE 327 AA; 34347 MW; 9C4CBF50F1C6F85D CRC64; MVPVSTENPF GQVLVALVTP FTADGEVDWA GVEKHMDDVI VAGADGIVVT GTTGETSTLT DPEKIKLVEV GRSVSAGRAK IITGGGSNET AHAMQLARQS EKAGADGNMI VTPYYNKPTQ AGVLTHFRMI ADATDLPVIL YDIPGRTGIP IQYETILRAA KHPNILAVKD AKGDLAQASR VLNQTGLMYF AGDDANALPT LAIGGTGLIG VTANITATPY RTMVDAVNAG DLAAATHAHQ QLEPLVRAVM THVPGTVAAK YILHGLGRIG SPRVRLPLVG PEEWEAAQIE DEIDPLRDVP GVDFRNFRPD RNAAAGGALP QVAGTTR //