UniProt: Q88VD7

Database: UniProt
Entry: Q88VD7_LACPN

LinkDB:  Q88VD7_LACPN 
Original site:  Q88VD7_LACPN

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (9)   
   EMBL (9)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   Q88VD7_LACPN            Unreviewed;       290 AA.
AC   Q88VD7; Q76H89;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 161.
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:BAD01034.1};
GN   Synonyms=dapA1 {ECO:0000313|EMBL:BBA83219.1}, dapA_1
GN   {ECO:0000313|EMBL:QHM48361.1}, dapA_2 {ECO:0000313|EMBL:QHM38144.1};
GN   ORFNames=ASV54_08525 {ECO:0000313|EMBL:APD01396.1}, AVR83_12095
GN   {ECO:0000313|EMBL:AOB23636.1}, C7M36_02454
GN   {ECO:0000313|EMBL:QHM38144.1}, C7M40_00284
GN   {ECO:0000313|EMBL:QHM48361.1}, Lp19_3517
GN   {ECO:0000313|EMBL:KZU92231.1}, LPJSA22_01958
GN   {ECO:0000313|EMBL:ODO61978.1}, LpLQ80_09475
GN   {ECO:0000313|EMBL:AWI40746.1}, SN35N_2840
GN   {ECO:0000313|EMBL:BBA83219.1};
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590 {ECO:0000313|EMBL:BAD01034.1};
RN   [1] {ECO:0000313|EMBL:BAD01034.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cahyanto M.N., Kawasaki H., Fujiyama K., Seki T.;
RT   "Cloning of Lactobacillus plantarum IAM 12477 lysine biosynthetic genes
RT   encoding functional aspartate semialdehyde dehydrogenase,
RT   dihydrodipicolinate synthase, and dihydrodipicolinate reductase.";
RL   J. Biosci. Bioeng. 22:409-416(2006).
RN   [2] {ECO:0000313|Proteomes:UP000183026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA   McLeod A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AOB23636.1, ECO:0000313|Proteomes:UP000093296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF {ECO:0000313|EMBL:AOB23636.1,
RC   ECO:0000313|Proteomes:UP000093296};
RA   Petkau K., Fast D., Duggal A., Foley E.;
RT   "Comparative evaluation of the genomes of common bacterial members of the
RT   Drosophila intestinal community.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KZU92231.1, ECO:0000313|Proteomes:UP000076882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19.1 {ECO:0000313|EMBL:KZU92231.1,
RC   ECO:0000313|Proteomes:UP000076882};
RA   Martino M.E.;
RT   "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT   uncoupling from niche constraints.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ODO61978.1, ECO:0000313|Proteomes:UP000094892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSA22 {ECO:0000313|EMBL:ODO61978.1,
RC   ECO:0000313|Proteomes:UP000094892};
RA   Choi H.S.;
RT   "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT   fermented soybean paste.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BBA83219.1, ECO:0000313|Proteomes:UP000269784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN35N {ECO:0000313|EMBL:BBA83219.1,
RC   ECO:0000313|Proteomes:UP000269784};
RX   PubMed=29607926; DOI=.1248/bpb.b17-00840;
RA   Noda M., Shiraga M., Kumagai T., Danshiitsoodol N., Sugiyama M.;
RT   "Characterization of the SN35N Strain-Specific Exopolysaccharide Encoded in
RT   the Whole Circular Genome of a Plant-Derived Lactobacillus plantarum.";
RL   Biol. Pharm. Bull. 41:536-545(2018).
RN   [7] {ECO:0000313|EMBL:QHM38144.1, ECO:0000313|Proteomes:UP000464882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRCM101167 {ECO:0000313|EMBL:QHM38144.1,
RC   ECO:0000313|Proteomes:UP000464882};
RA   Jeong D.-Y.;
RT   "Lactobacillus plantatrum SRCM101167 having anti-virus activity species
RT   isolated from Korea kimchi.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:QHM48361.1, ECO:0000313|Proteomes:UP000465032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM48361.1,
RC   ECO:0000313|Proteomes:UP000465032};
RA   Jeong D.-Y.;
RT   "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT   isolated from Korea kimchi.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AWI40746.1, ECO:0000313|Proteomes:UP000244922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LQ80 {ECO:0000313|EMBL:AWI40746.1,
RC   ECO:0000313|Proteomes:UP000244922};
RA   Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA   Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA   Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA   Cai Y., Suzuki C.;
RT   "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT   for Preparation of Fermented Liquid Feed for Pig.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:APD01396.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MF1298 {ECO:0000313|EMBL:APD01396.1};
RA   McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (AUG-2018) 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; CP013753; AOB23636.1; -; Genomic_DNA.
DR   EMBL; CP013149; APD01396.1; -; Genomic_DNA.
DR   EMBL; CP028977; AWI40746.1; -; Genomic_DNA.
DR   EMBL; AB101670; BAD01034.1; -; Genomic_DNA.
DR   EMBL; AP018405; BBA83219.1; -; Genomic_DNA.
DR   EMBL; LUXM01000040; KZU92231.1; -; Genomic_DNA.
DR   EMBL; MCOL01000001; ODO61978.1; -; Genomic_DNA.
DR   EMBL; CP028334; QHM38144.1; -; Genomic_DNA.
DR   EMBL; CP028241; QHM48361.1; -; Genomic_DNA.
DR   RefSeq; WP_003640801.1; NZ_WYDR01000012.1.
DR   KEGG; lpb:SH83_09010; -.
DR   PATRIC; fig|1590.142.peg.1944; -.
DR   OMA; GMDACVP; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000076882; Unassembled WGS sequence.
DR   Proteomes; UP000093296; Chromosome.
DR   Proteomes; UP000094892; Unassembled WGS sequence.
DR   Proteomes; UP000183026; Chromosome.
DR   Proteomes; UP000244922; Chromosome.
DR   Proteomes; UP000269784; Chromosome.
DR   Proteomes; UP000464882; Chromosome.
DR   Proteomes; UP000465032; 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   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
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; 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};
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        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         48
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            47
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   290 AA;  30593 MW;  2C57C1478688EED2 CRC64;
     MNFANVDLMT AMVTPFDDHQ QLDEKRLASL IEHLLAHGTQ GILVGGTTGE APTLTEDEKL
     TLLKKAAEIV DGRVPIVAGT GSNSTAATIA FTKKVSQIKG IDAALVVVPY YNKPDQAGMI
     AHFTAVADQG GLPVIIYNIP GRVIVKMTVA TILTLAQNPN IIGIKQCATM EEFGAIVENA
     PADFLVYTGE DSQSLAAKEI GGAGVISVAS HIYGDEMTAM FSAIDQGEIA TAAKYQRDLT
     PKMSALFSAP SPSPVKAALN HLGQPVGEPR LPILPLSTEQ TAQLFKTLNI
//

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