DAPA_SACD2
ID DAPA_SACD2 Reviewed; 291 AA.
AC Q21HE7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; OrderedLocusNames=Sde_2622;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
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:0000305}.
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DR EMBL; CP000282; ABD81882.1; -; Genomic_DNA.
DR RefSeq; WP_011469099.1; NC_007912.1.
DR AlphaFoldDB; Q21HE7; -.
DR SMR; Q21HE7; -.
DR STRING; 203122.Sde_2622; -.
DR EnsemblBacteria; ABD81882; ABD81882; Sde_2622.
DR KEGG; sde:Sde_2622; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_6; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1438588at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000001947; 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; -; 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 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.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lyase;
KW Lysine biosynthesis; Reference proteome; Schiff base.
FT CHAIN 1..291
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_1000050260"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 161
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 45
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 203
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 44
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 107
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
SQ SEQUENCE 291 AA; 30725 MW; 7122C23A14DB9ABA CRC64;
MLRGSMVALV TPMQADGSLD WEALHKLVDW HLQEGTDAIV AVGTTGESAT LDVKEHIAVI
RAVVDQVNGR VPVIAGTGAN STSEAIELTQ AAKDGGVDAC LLVAPYYNKP TQEGLFLHHQ
KIAASVAIPQ LLYNVPGRTA VDMLPETIVR LSHVDNIVGV KEATGDIARV GQILESAKAG
FLLISGDDDT AVDFIAAGGV GEISVTANVA PKLVAQMCEL AAQGKVEEAR AINARLADVH
TAMFLESNPI PVKWALAKMG LMPNGIRLPL TPLDAKYHLQ VEQALRAANL L
