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Database: UniProt
Entry: W0V1Z7_9BURK
LinkDB: W0V1Z7_9BURK
Original site: W0V1Z7_9BURK 
ID   W0V1Z7_9BURK            Unreviewed;       350 AA.
AC   W0V1Z7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ECO:0000313|EMBL:CDG81358.1};
GN   ORFNames=GJA_699 {ECO:0000313|EMBL:CDG81358.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG81358.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG81358.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00418}.
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DR   EMBL; HG322949; CDG81358.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0V1Z7; -.
DR   STRING; 1349767.GJA_699; -.
DR   KEGG; jag:GJA_699; -.
DR   PATRIC; fig|1349767.4.peg.2411; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_7_1_4; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000027604; Chromosome I.
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:SF15; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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}; Cytoplasm {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}; Reference proteome {ECO:0000313|Proteomes:UP000027604};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00418}.
FT   ACT_SITE        153
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        181
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         65
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         221
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   SITE            64
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT   SITE            127
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   350 AA;  37513 MW;  BCE395413BA858F3 CRC64;
     MTPLMHPPIR DNAMSSSRIT GHFQGIWVPL VTPFDDGEVD LEAAQRLAAE LVASGIHGLV
     VCGTTGEAAM LSEREQALLL DAVLETVGPH FPVVMGAGGS DTRAVAASVK RFDDHPLAGL
     LISAPSYVRP SQEGILRHFQ AISAATDHSI VLYNIPARTG INIEPATVAE LSRDTRFVAI
     KEAGGNVLQI TDLLLNTRLD VLSGDDTLLL ATLRMGGHGA MSAAAHLRPD LYVQLYELVK
     TGQIAAAQEL FKSLLPVIRL LFAEPNPAPV KAALAMLGKL KDELRLPMTC MSAAGKARLF
     SALDDLMAIP EWHTPAEDKH HASQGWLLQL VSSSPSLVVP AGRYDDHHHN
//
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