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Database: UniProt
Entry: A0A0P9EBC9_9ARCH
LinkDB: A0A0P9EBC9_9ARCH
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ID   A0A0P9EBC9_9ARCH        Unreviewed;       296 AA.
AC   A0A0P9EBC9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:KPV63996.1};
GN   ORFNames=AOA65_1122 {ECO:0000313|EMBL:KPV63996.1};
OS   Candidatus Bathyarchaeota archaeon BA1.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV63996.1, ECO:0000313|Proteomes:UP000050312};
RN   [1] {ECO:0000313|EMBL:KPV63996.1, ECO:0000313|Proteomes:UP000050312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA1 {ECO:0000313|EMBL:KPV63996.1};
RX   PubMed=26494757; DOI=10.1126/science.aac7745;
RA   Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA   Golding S.D., Tyson G.W.;
RT   "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT   genome-centric metagenomics.";
RL   Science 350:434-438(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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00418}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPV63996.1}.
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; LIHJ01000043; KPV63996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9EBC9; -.
DR   STRING; 1700835.AOA65_1122; -.
DR   KEGG; barc:AOA65_1122; -.
DR   PATRIC; fig|1700835.3.peg.1625; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000050312; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProt.
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; cd00408; DHDPS-like; 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: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; 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}; Lyase {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        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         208
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            48
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT   SITE            111
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   296 AA;  32001 MW;  8AFBBDB0F37FF80D CRC64;
     MSKLKLEGIF PPHITPFTRE GEVNEEALRT CINFWIESGV SGLVPCGSNG EAPYLSREER
     KRVIGTVIDE INGKVPVITG TGGISTRETI ALTKDAKDLG ADAALVVTPF YFKLSNKEIY
     EHYRAVMEAA DLPIIVYNVP KFTGFSLDPI VISQLASKYE NVIGVKDSSG SIAQITEIIR
     LVGNKISVMA GTADGVLPTL MLGGKGAIVA VANVAPKLCV DLYKAFKEGN YGEASRIQLQ
     IYHLNEVLVK KHNQLSAIKE ALNVMGLPGG YPRRPALPLD EEGKGEIKKI LGSYLS
//
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