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Database: UniProt
Entry: A0A014N606_9GAMM
LinkDB: A0A014N606_9GAMM
Original site: A0A014N606_9GAMM 
ID   A0A014N606_9GAMM        Unreviewed;       294 AA.
AC   A0A014N606;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=BG55_13895 {ECO:0000313|EMBL:EXU74828.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU74828.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU74828.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU74828.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-2014) 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: 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:EXU74828.1}.
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; JFHN01000053; EXU74828.1; -; Genomic_DNA.
DR   RefSeq; WP_034938310.1; NZ_VFIK01000001.1.
DR   AlphaFoldDB; A0A014N606; -.
DR   STRING; 69222.BG55_13895; -.
DR   PATRIC; fig|69222.5.peg.2853; -.
DR   OrthoDB; 9782828at2; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000019918; Unassembled WGS sequence.
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:SF66; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 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};
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:UP000019918};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00418}.
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        161
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         45
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         203
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            44
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT   SITE            107
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   294 AA;  31597 MW;  33C24C9C809289F4 CRC64;
     MFTGSIVALI TPMDDKGYVC RASLKKLIDY HVASGTSAIV SVGTTGESAT LSHDEHGDVV
     KMTLELADGR IPVIAGTGAN ATAEGISLTR QFEKSGVVGC LTVTPYYNRP TQEGLYQHFK
     AIAESTDLPQ MLYNVPSRTG CDMLPETVGR LAKIKNIIGI KEATGNLSRV SQIQELVDDD
     FILVSGDDGT ALDFMQLGGR GVISVTANIA AREMVQVCTL AQQGNFAEAR RLNQRLMPLH
     QKLFIEPNPV PVKWAAKKLG LIATDTLRLP MTPMTDAGRP VVEQALKCAG LLEI
//
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