ID Q54A52_LACLL Unreviewed; 297 AA.
AC Q54A52;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
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:BAD11368.1};
GN ORFNames=HPC60_03600 {ECO:0000313|EMBL:QLF89832.1}, JCM5805K_2059
GN {ECO:0000313|EMBL:GAM80943.1}, LKF24_0569
GN {ECO:0000313|EMBL:KST99094.1}, LL275_1654
GN {ECO:0000313|EMBL:ARD99281.1}, LLUC77_1772
GN {ECO:0000313|EMBL:ARE08885.1}, M20_1359 {ECO:0000313|EMBL:KSU20729.1};
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360 {ECO:0000313|EMBL:BAD11368.1};
RN [1] {ECO:0000313|EMBL:BAD11368.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IAM 1198 {ECO:0000313|EMBL:BAD11368.1};
RA Cahyanto M.N., Kawasaki H., Fujiyama K., Seki T.;
RT "Cloning and Expression in Escherichia coli of Lysine Biosynthetic Genes
RT from Lactic Acid Bacterium Lactococcus lactis spp. lactis IAM1198.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM80943.1, ECO:0000313|Proteomes:UP000031847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 5805 {ECO:0000313|EMBL:GAM80943.1,
RC ECO:0000313|Proteomes:UP000031847};
RA Fujii T., Tomita Y., Ikushima S., Fujiwara D.;
RT "Lactococcus lactis subsp.lactis JCM 5805 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000053719, ECO:0000313|Proteomes:UP000053856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF24 {ECO:0000313|Proteomes:UP000053856}, and M20
RC {ECO:0000313|Proteomes:UP000053719};
RA Wels M., Backus L., Boekhorst J., Dijkstra A., Beerthuizen M., Kelly W.,
RA Siezen R., Bachmann H., Van Hijum S.;
RT "Draft Genome Sequences of 11 Lactococcus lactis subspecies cremoris
RT strains.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000191916, ECO:0000313|Proteomes:UP000192085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=275 {ECO:0000313|EMBL:ARD99281.1,
RC ECO:0000313|Proteomes:UP000192085}, and UC77
RC {ECO:0000313|EMBL:ARE08885.1, ECO:0000313|Proteomes:UP000191916};
RX PubMed=28356072; DOI=.1186/s12864-017-3650-5;
RA Kelleher P., Bottacini F., Mahony J., Kilcawley K.N., van Sinderen D.;
RT "Comparative and functional genomics of the Lactococcus lactis taxon;
RT insights into evolution and niche adaptation.";
RL BMC Genomics 18:267-267(2017).
RN [5] {ECO:0000313|EMBL:KST99094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KF24 {ECO:0000313|EMBL:KST99094.1}, and M20
RC {ECO:0000313|EMBL:KSU20729.1};
RX PubMed=28360177;
RA Backus L., Wels M., Boekhorst J., Dijkstra A.R., Beerthuyzen M.,
RA Kelly W.J., Siezen R.J., van Hijum S.A., Bachmann H.;
RT "Draft Genome Sequences of 24 Lactococcus lactis Strains.";
RL Genome Announc. 5:e01737-e01716(2017).
RN [6] {ECO:0000313|Proteomes:UP000509769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G121 {ECO:0000313|Proteomes:UP000509769};
RA Wang Z., Minarsch E.-M., Kublik S., Heine H., Schloter M., Foesel B.;
RT "Complete Genome Sequence of Lactococcus lactis subsp. lactis G121, an
RT isolate with allergy-protective traits derived from a farming
RT environment.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QLF89832.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G121 {ECO:0000313|EMBL:QLF89832.1};
RA Wang Z., Minarsch E.-M., Kublik S., Heine H., Schloter M., Foesel B.;
RT "Complete Genome Sequence of Lactococcus lactis subsp. lactis G121, an
RT isolate with allergy-protective traits derived from a farming
RT environment.";
RL Submitted (SEP-2020) 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; CP015897; ARD99281.1; -; Genomic_DNA.
DR EMBL; CP015906; ARE08885.1; -; Genomic_DNA.
DR EMBL; AB090276; BAD11368.1; -; Genomic_DNA.
DR EMBL; BBSI01000033; GAM80943.1; -; Genomic_DNA.
DR EMBL; LKLH01000038; KST99094.1; -; Genomic_DNA.
DR EMBL; LKLU01000081; KSU20729.1; -; Genomic_DNA.
DR EMBL; CP053671; QLF89832.1; -; Genomic_DNA.
DR RefSeq; WP_003129414.1; NZ_WUBD01000013.1.
DR PATRIC; fig|1360.100.peg.1512; -.
DR OMA; GMDACVP; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000031847; Unassembled WGS sequence.
DR Proteomes; UP000053719; Unassembled WGS sequence.
DR Proteomes; UP000053856; Unassembled WGS sequence.
DR Proteomes; UP000191916; Chromosome.
DR Proteomes; UP000192085; Chromosome.
DR Proteomes; UP000509769; 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 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; 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 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 172
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 55
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 54
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 118
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 297 AA; 32190 MW; CE8C2449ABEBCD84 CRC64;
MSAKETIEKL QNARIITALV TPFKENGQIN FGAFPKLIED LLANHTEGLI LAGTTAESPT
LTHDEELAIF AAVNKIVDGR IPLIAGVGTN DTRDSVEFVK EVAELGYIDA GLAVTPYYNK
PSQEGIYQHF KAIATASDLP IILYNIPGRV VTEIQVETIL RLAELENVIA IKECTNTDNL
AYLIEKLPKD FLVYTGEDGL AFHTKALGGQ GVISVASHIL GQEFFEMFAE IDQGSIQKAA
AIQRKILPKI NALFSVTSPA PIKTVLNAKG YEVGGLRLPL VACTTEESKI ILEKIGN
//
