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 31-MAY-2011, entry version 14. DE RecName: Full=Dihydrodipicolinate synthase; DE Short=DHDPS; DE EC=4.2.1.52; GN Name=dapA; OrderedLocusNames=A2cp1_4217; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; 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 -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + pyruvate = CC dihydrodipicolinate + 2 H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the DHDPS family. 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; YP_002494600.1; NC_011891.1. DR ProteinModelPortal; B8JAN5; -. DR SMR; B8JAN5; 4-292. DR GeneID; 7297871; -. DR GenomeReviews; CP001359_GR; A2cp1_4217. DR KEGG; acp:A2cp1_4217; -. DR HOGENOM; HBG358848; -. DR ProtClustDB; PRK03170; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:dihydrodipicolinate synthase activity; IEA:EC. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00418; DapA; 1; -. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002220; Dihydrodipicolinate_synth-like. DR InterPro; IPR020625; Dihydrodipicolinate_synth_AS. DR InterPro; IPR020624; Dihydrodipicolinate_synth_CS. DR InterPro; IPR005263; Dihydrodipicolinate_synth_DapA. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR12128; DHDPS; 1. DR Pfam; PF00701; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. 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 Dihydrodipicolinate synthase. FT /FTId=PRO_1000134855. FT ACT_SITE 162 162 Schiff-base intermediate with substrate FT (By similarity). FT SITE 134 134 Involved in proton transfer during FT cleavage (By similarity). 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 //