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   01-MAY-2013, entry version 30.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase;
DE            Short=HTPA synthase;
DE            EC=4.3.3.7;
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   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-
CC       semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)-
CC       4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + 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; dimer of dimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DapA family.
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 (PubMed:8993314 and
CC       PubMed:20503968) that the product of the enzymatic reaction is not
CC       dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-
CC       (2S)-dipicolinic acid (HTPA), and that the consecutive dehydration
CC       reaction leading to DHDP is not spontaneous but catalyzed by DapB
CC       (PubMed:20503968).
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DR   EMBL; CP001359; ACL67534.1; -; Genomic_DNA.
DR   RefSeq; YP_002494600.1; NC_011891.1.
DR   ProteinModelPortal; B8JAN5; -.
DR   STRING; 455488.A2cp1_4217; -.
DR   EnsemblBacteria; ACL67534; ACL67534; A2cp1_4217.
DR   GeneID; 7297871; -.
DR   KEGG; acp:A2cp1_4217; -.
DR   PATRIC; 20915390; VBIAnaDeh28364_4253.
DR   eggNOG; COG0329; -.
DR   HOGENOM; HOG000173604; -.
DR   KO; K01714; -.
DR   OMA; ADAILCV; -.
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:4-hydroxy-tetrahydrodipicolinate synthase; IEA:EC.
DR   GO; GO:0016843; F:amine-lyase activity; IEA:HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 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       4-hydroxy-tetrahydrodipicolinate
FT                                synthase.
FT                                /FTId=PRO_1000134855.
FT   ACT_SITE    134    134       Proton donor/acceptor (By similarity).
FT   ACT_SITE    162    162       Schiff-base intermediate with substrate
FT                                (By similarity).
FT   BINDING      46     46       Pyruvate (By similarity).
FT   BINDING     205    205       Pyruvate; via carbonyl oxygen (By
FT                                similarity).
FT   SITE         45     45       Part of a proton relay during catalysis
FT                                (By similarity).
FT   SITE        108    108       Part of a proton relay during catalysis
FT                                (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
//