ID A0A1X0WA37_9GAMM Unreviewed; 293 AA. AC A0A1X0WA37; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 02-DEC-2020, entry version 15. 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 ORFNames=BS640_20280 {ECO:0000313|EMBL:ORJ23658.1}; OS Rouxiella badensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rouxiella. OX NCBI_TaxID=1646377 {ECO:0000313|EMBL:ORJ23658.1, ECO:0000313|Proteomes:UP000192536}; RN [1] {ECO:0000313|EMBL:ORJ23658.1, ECO:0000313|Proteomes:UP000192536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 100043 {ECO:0000313|EMBL:ORJ23658.1, RC ECO:0000313|Proteomes:UP000192536}; RX PubMed=28100296; DOI=10.1099/ijsem.0.001794; RA Le Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C., Hausmann R., RA Lomprez F., Vandenbogaert M., Manuguerra J.C., Grimont P.A.; RT "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated from RT peat bog soil in Germany and emendation of the genus description."; RL Int. J. Syst. Evol. Microbiol. 67:1255-1259(2017). 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-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: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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ORJ23658.1}. 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; MRWE01000046; ORJ23658.1; -; Genomic_DNA. DR RefSeq; WP_017493199.1; NZ_MRWE01000046.1. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000192536; Unassembled WGS sequence. 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; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00418}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418}; KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_00418}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_00418}; Reference proteome {ECO:0000313|Proteomes:UP000192536}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00418}. FT ACT_SITE 133 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT ACT_SITE 161 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT BINDING 45 FT /note="Pyruvate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT BINDING 204 FT /note="Pyruvate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 44 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 107 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" SQ SEQUENCE 293 AA; 31195 MW; 491504C7A439F47D CRC64; MFTGSIVALV TPMDDKGAVC RASLKKLIDY HVSSGTAAIV SVGTTGESAT LNHDEHADVV LQTLELADGR IPVIAGTGAN ATAEAIALTQ RFENSGVVGC LTVTPYYNRP TQEGLYQHFK AIAESTALPQ ILYNVPSRTG CDMLPATIAR LAKIKNIVAC KEATGNLSRV SQIQVLVDDE DFILLSGDDF SGLDFMQLGG KGVISVTANI AAAEMVELCR LAAEGKFAEA RRLNQRLMPL HQHLFVEANP IPVKWACKAL GLIATDTVRL PMTPLTDAAR PIVEDALIKA GLL //