ID Q7UVB1_RHOBA Unreviewed; 314 AA.
AC Q7UVB1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 128.
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:CAD72814.1};
GN OrderedLocusNames=RB2746 {ECO:0000313|EMBL:CAD72814.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD72814.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD72814.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294137; CAD72814.1; -; Genomic_DNA.
DR RefSeq; NP_865130.1; NC_005027.1.
DR AlphaFoldDB; Q7UVB1; -.
DR STRING; 243090.RB2746; -.
DR EnsemblBacteria; CAD72814; CAD72814; RB2746.
DR KEGG; rba:RB2746; -.
DR PATRIC; fig|243090.15.peg.1263; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_0; -.
DR InParanoid; Q7UVB1; -.
DR OrthoDB; 9782828at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
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 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00418}.
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 57
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 213
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 56
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 119
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 314 AA; 33439 MW; EE59408F1B09F253 CRC64;
MFRTCLMSPR KGSDFAGLST AIVTPFRDGQ VDEKRLAEQI DFQIDSGVTC IVPCGTTGES
PTLTHDEHER VISLTIQHVA GRVKVMAGTG SNSTAEALRL TRRAADEGAD ATLQVAPYYN
KPTQEGMYQH FRAVAEAVDI PVCVYNIPGR SAKNIEVDTI VRLAELPNIT MVKEATGSLD
QCTAVLGATN LTVLSGDDSL TLPMMSVGAE GVISVAANLV PSVLLEMVQT AAAGDYTKAA
ELHHRLYSLC SKMLGLATNP IPVKAAMQMV GRDTGEMRLP MVPLDDADRA ILQETLMKFG
MESAIAGQLQ ASGA
//
