ID A0A1X0WA37_9GAMM Unreviewed; 293 AA. AC A0A1X0WA37; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 28-FEB-2018, entry version 4. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {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; RA LE Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C., RA Hausmann R., Lomprez F., Vandenbogaert M., Manuguerra J.C., RA Grimont P.A.; RT "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated RT from peat bog soil in Germany and emendation of the genus RT description."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2017). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000256|HAMAP-Rule:MF_00418, CC ECO:0000256|SAAS:SAAS00570606}. CC -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)- CC 4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00570589}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00570584}. 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. CC {ECO:0000256|PIRNR:PIRNR001365, ECO:0000256|SAAS:SAAS00579284}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ORJ23658.1}. 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:0000256|HAMAP- CC 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; 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|HAMAP-Rule:MF_00418, KW ECO:0000256|SAAS:SAAS00570585}; KW Complete proteome {ECO:0000313|Proteomes:UP000192536}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418, KW ECO:0000256|SAAS:SAAS00570604}; KW Lyase {ECO:0000256|PIRNR:PIRNR001365, ECO:0000256|SAAS:SAAS00579236}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418, KW ECO:0000256|SAAS:SAAS00570598}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00418, KW ECO:0000256|SAAS:SAAS00570587}. FT ACT_SITE 133 133 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00418}. FT ACT_SITE 161 161 Schiff-base intermediate with substrate. FT {ECO:0000256|HAMAP-Rule:MF_00418}. FT BINDING 45 45 Pyruvate. {ECO:0000256|HAMAP-Rule: FT MF_00418}. FT BINDING 204 204 Pyruvate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00418}. FT SITE 44 44 Part of a proton relay during catalysis. FT {ECO:0000256|HAMAP-Rule:MF_00418}. FT SITE 107 107 Part of a proton relay during catalysis. FT {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 //