ID A0A068NEZ4_9ACTO Unreviewed; 302 AA. AC A0A068NEZ4; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 24-JAN-2024, entry version 40. 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=FB03_00765 {ECO:0000313|EMBL:AIE82046.1}; OS Actinotignum schaalii. OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae; OC Actinotignum. OX NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82046.1, ECO:0000313|Proteomes:UP000035032}; RN [1] {ECO:0000313|EMBL:AIE82046.1, ECO:0000313|Proteomes:UP000035032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82046.1, RC ECO:0000313|Proteomes:UP000035032}; RX PubMed=25189588; RA Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M., RA Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M., RA Christensen J.J., Prag J., Thomsen T.R.; RT "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420."; RL Genome Announc. 2:e00880-14(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 + H(+) + H2O; 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: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: 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; CP008802; AIE82046.1; -; Genomic_DNA. DR RefSeq; WP_026428560.1; NZ_CP008802.1. DR AlphaFoldDB; A0A068NEZ4; -. DR GeneID; 81701036; -. DR KEGG; asg:FB03_00765; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000035032; 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; 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-TETRAHYDRODIPICOLINATE SYNTHASE; 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}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00418}. FT ACT_SITE 142 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT ACT_SITE 170 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418, FT ECO:0000256|PIRSR:PIRSR001365-1" FT BINDING 54 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 210 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 53 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" FT SITE 116 FT /note="Part of a proton relay during catalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418" SQ SEQUENCE 302 AA; 31422 MW; 52935AA17130DB21 CRC64; MDEHTLPSRS FGSVSVAMVT PFHADGSLDV DAAVALATTL VDQGCDALLL SGTTGESPTT HQPEKDVLVR EVCAAVRNRA MVIAGAGSND TAHAVRIARG AEKSGAQGLL VVAPYYNRPS QEGVYQHILN VTEATDLPVM VYDIPGRTGV RLELDTLLRL AEHPRILAVK DATGDVAGGF VKMARTGLEY YSGDDALNFA WLAHGASGVI SVAGHVIAAR LRALVEQVDA GDLPAARREA AAQRHIISAI MGSGQGAVMA KEALKLLGVI PSATLRLPLV GASAVQIAEL AEALRAEGLL AD //