ID DAPA_ANAD2 Reviewed; 295 AA. AC B8JAN5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 05-DEC-2018, entry version 55. 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=A2cp1_4217; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {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; CC EC=4.3.3.7; 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 CC synthase (DHDPS), catalyzing the condensation of (S)-aspartate- CC beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate CC (DHDP). However, it was shown in E.coli that the product of the CC enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4- CC hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that CC the consecutive dehydration reaction leading to DHDP is not CC spontaneous but catalyzed by DapB. {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; CP001359; ACL67534.1; -; Genomic_DNA. DR RefSeq; WP_015935245.1; NC_011891.1. DR ProteinModelPortal; B8JAN5; -. DR SMR; B8JAN5; -. DR EnsemblBacteria; ACL67534; ACL67534; A2cp1_4217. DR KEGG; acp:A2cp1_4217; -. DR HOGENOM; HOG000173604; -. DR KO; K01714; -. DR OMA; GMDACVP; -. DR OrthoDB; POG091H00C1; -. DR BioCyc; ADEH455488:G1GUO-4265-MONOMER; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; 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; -; 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 PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; Schiff base. FT CHAIN 1 295 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_1000134855. FT ACT_SITE 134 134 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT ACT_SITE 162 162 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT BINDING 46 46 Pyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00418}. FT BINDING 205 205 Pyruvate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 45 45 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 108 108 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. SQ SEQUENCE 295 AA; 31069 MW; CED52E094FD83290 CRC64; MRRLEGSMVA IVTPMKDGAV DLRALRDLTE WQLAEGTDGI VPCGTTGEGV TLTPAERADV IRTVIETVRG RALVIAGAGS NATHEAIESV KLAKTLGADA ALVVTPYYNK PTQEGLFRHY QAIWEATRFP VVAYNVPSRT SVDLLPETVA RLAKAGAIAG IKEATANMDR QVQLVEKVGK DAIAYLSGDD FTVLPYIACG GHGVISVIAN VAPRAMKELV VAARSGDLAG ALAKQAAMAE LNRMMFVETN PGPVKAAVAL LGRSGGELRL PLAPVSEASL AKVRDAMVRF GLKLA //