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   28-NOV-2012, entry version 25.
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.
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DR   EMBL; CP001359; ACL67534.1; -; Genomic_DNA.
DR   RefSeq; YP_002494600.1; NC_011891.1.
DR   ProteinModelPortal; B8JAN5; -.
DR   STRING; B8JAN5; -.
DR   GeneID; 7297871; -.
DR   GenomeReviews; CP001359_GR; A2cp1_4217.
DR   KEGG; acp:A2cp1_4217; -.
DR   PATRIC; 20915390; VBIAnaDeh28364_4253.
DR   eggNOG; COG0329; -.
DR   HOGENOM; HOG000173604; -.
DR   KO; K01714; -.
DR   OMA; GMDACVP; -.
DR   ProtClustDB; PRK03170; -.
DR   BioCyc; ADEH455488:GH35-4273-MONOMER; -.
DR   UniPathway; UPA00034; UER00017.
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   Gene3D; 3.20.20.70; Aldolase_TIM; 1.
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   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; 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
//