ID Q17ZX0_CLOD6 Unreviewed; 295 AA. AC Q17ZX0; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 02-SEP-2026, entry version 131. 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=dapA3 {ECO:0000313|EMBL:CAJ70123.1}; GN Synonyms=dapA {ECO:0000256|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=CD630_32250 {ECO:0000313|EMBL:CAJ70123.1}; OS Clostridioides difficile (strain 630) (Peptoclostridium difficile). OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales; OC Peptostreptococcaceae; Clostridioides. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ70123.1, ECO:0000313|Proteomes:UP000001978}; RN [1] {ECO:0000313|EMBL:CAJ70123.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70123.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L., RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a highly RT mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). RN [2] {ECO:0000313|EMBL:CAJ70123.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70123.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=21349987; DOI=10.1099/jmm.0.030452-0; RA Monot M., Boursaux-Eude C., Thibonnier M., Vallenet D., Moszer I., RA Medigue C., Martin-Verstraete I., Dupuy B.; RT "Reannotation of the genome sequence of Clostridium difficile strain 630."; RL J. Med. Microbiol. 60:1193-1199(2011). RN [3] {ECO:0000313|EMBL:CAJ70123.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70123.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=24568651; DOI=10.1186/1471-2164-15-160; RA Pettit L.J., Browne H.P., Yu L., Smits W.K., Fagan R.P., Barquist L., RA Martin M.J., Goulding D., Duncan S.H., Flint H.J., Dougan G., RA Choudhary J.S., Lawley T.D.; RT "Functional genomics reveals that Clostridium difficile Spo0A coordinates RT sporulation, virulence and metabolism."; RL BMC Genomics 15:160-160(2014). 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; AM180355; CAJ70123.1; -; Genomic_DNA. DR RefSeq; WP_003422063.1; NC_009089.1. DR AlphaFoldDB; Q17ZX0; -. DR STRING; 272563.CD630_32250; -. DR EnsemblBacteria; CAJ70123; CAJ70123; CD630_32250. DR GeneID; 66355644; -. DR KEGG; cdf:CD630_32250; -. DR KEGG; pdc:CDIF630_03521; -. DR PATRIC; fig|272563.120.peg.3406; -. DR eggNOG; COG0329; Bacteria. DR OrthoDB; 9782828at2; -. DR PhylomeDB; Q17ZX0; -. DR BioCyc; PDIF272563:G12WB-3392-MONOMER; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000001978; 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 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 {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:UP000001978}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00418}. FT ACT_SITE 134 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT ACT_SITE 162 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT BINDING 46 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 204 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 45 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 108 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" SQ SEQUENCE 295 AA; 31595 MW; A747CDE67412FD9C CRC64; MIFKGSAVAL VTPFTKDNKV DFDKLGELVE YQIANGTDAI VSCGTTGEAN TMTDEEQLAT IKYVVEKVNK RVPVIAGSGS NDTMHSVNLS QEAEKLGVDA LLIITPYYNK ANKAGLKRHF ETIANSVKLP IILYNVPGRT CVNISPSLIV ELAKIDNIVA VKEASGDLGQ VAEIASLVPD DFAIYSGNDD TILPLLSLGG QGVISVLANV CPQETHDLVA KFFEGDIEGS RKLQLGMDAL IAALFIEVNP IPVKTAMNLL GFNVGDLRLP LAEMDPANLE VLKKELVNFG LKVNA //