ID I3Z094_AEQSU Unreviewed; 291 AA.
AC I3Z094;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=Aeqsu_3233 {ECO:0000313|EMBL:AFL82662.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL82662.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL82662.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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: 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; CP003280; AFL82662.1; -; Genomic_DNA.
DR RefSeq; WP_014783911.1; NC_018013.1.
DR AlphaFoldDB; I3Z094; -.
DR STRING; 746697.Aeqsu_3233; -.
DR KEGG; asl:Aeqsu_3233; -.
DR PATRIC; fig|746697.3.peg.3284; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_0_10; -.
DR OrthoDB; 9782828at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000006049; 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; 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 NCBIfam; TIGR00674; dapA; 1.
DR PANTHER; PTHR12128:SF72; 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; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00418};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00418}.
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 47
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 206
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 46
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 109
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 291 AA; 31188 MW; F607916C88509A6D CRC64;
MKELIGTGVA LITPFKSDFS VDVEGLKNVV NFNIENGINY LVVLGTTAES ATLSKEEKQV
VIDTIISANN GRLPLVLGIG GNNTQEVIAE MQTRDLSAFT AILSVSPYYN KPTQEGIYQH
FAAIAKAAPL PIILYNVPGR TASNVLPETV IRLANDFEKI VAIKEAAGDI VQAMKLISGC
PKEFLVISGD DMITLPIILA GGAGVISVIG EGFPKEFSKM VKLGLDKKAD EAYQIHYKIA
PAIDYIFAEG NPAGIKAVFK SLEICGDTVR LPLVGVSDGL RAKIDSFTRN F
//
