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Database: UniProt
Entry: A0A0M2SXW5_9BACI
LinkDB: A0A0M2SXW5_9BACI
Original site: A0A0M2SXW5_9BACI 
ID   A0A0M2SXW5_9BACI        Unreviewed;       306 AA.
AC   A0A0M2SXW5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE            EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
GN   ORFNames=WQ57_04040 {ECO:0000313|EMBL:KKK39404.1};
OS   Mesobacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK39404.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK39404.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK39404.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT   a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) 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}.
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};
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}.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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:KKK39404.1}.
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DR   EMBL; LAYY01000003; KKK39404.1; -; Genomic_DNA.
DR   RefSeq; WP_046522439.1; NZ_LAYY01000003.1.
DR   AlphaFoldDB; A0A0M2SXW5; -.
DR   PATRIC; fig|1408103.3.peg.914; -.
DR   OrthoDB; 9771791at2; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000034166; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
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   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:SF28; 2-DEHYDRO-3-DEOXY-D-GLUCONATE ALDOLASE YAGE-RELATED; 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};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        167
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         212
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   306 AA;  33812 MW;  78DE3C2C11F2D331 CRC64;
     MAATNLFTGI IPPVSTIFNK DGKLDQAGMS LLINDLISRG VNGLFFLGTG GEFSQLTIEE
     RKEVAEFAVK EVNGRVPVLI GTGALNTKTV IELNKHAKAI QADGVVVVNP YYLTLSEENL
     YRHYSEIAEH TELPILLYNF PALTGQNLSA NLVLRLVNQY NHIVGIKETV EKIGHIREII
     LKVKSGNPEF RVLCGYEDLF LDTLTLGGDG IIGAGCNFAP ELSIDLYDAF LRGDYQKAVE
     LNKRLAMIPE MYKLDTPFIN VIKEAIAMSG LDISTEVLPP VRPLDEEKKK ELENILKQAE
     ILAKNV
//
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