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 11-DEC-2019, entry version 59. 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=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., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA 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-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-hydroxy- CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC 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; CP001359; ACL67534.1; -; Genomic_DNA. DR RefSeq; WP_015935245.1; NC_011891.1. DR SMR; B8JAN5; -. DR EnsemblBacteria; ACL67534; ACL67534; A2cp1_4217. DR KEGG; acp:A2cp1_4217; -. DR HOGENOM; HOG000173604; -. DR KO; K01714; -. DR OMA; GMDACVP; -. 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 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; -; 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; Cytoplasm; Diaminopimelate biosynthesis; Lyase; KW Lysine biosynthesis; Schiff base. FT CHAIN 1..295 FT /note="4-hydroxy-tetrahydrodipicolinate synthase" FT /id="PRO_1000134855" FT ACT_SITE 134 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT ACT_SITE 162 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 46 FT /note="Pyruvate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT BINDING 205 FT /note="Pyruvate; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 45 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418" FT SITE 108 FT /note="Part of a proton relay during catalysis" FT /evidence="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 //