ID V2Q4D4_9BACT Unreviewed; 294 AA.
AC V2Q4D4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:USF23642.1};
GN ORFNames=N508_000707 {ECO:0000313|EMBL:USF23642.1}, N508_00167
GN {ECO:0000313|EMBL:ESJ99867.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ99867.1};
RN [1] {ECO:0000313|EMBL:ESJ99867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ99867.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23642.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23642.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) 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; AYGZ01000005; ESJ99867.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23642.1; -; Genomic_DNA.
DR RefSeq; WP_023275015.1; NZ_FTRD01000002.1.
DR AlphaFoldDB; V2Q4D4; -.
DR STRING; 1379858.N508_00167; -.
DR GeneID; 78587441; -.
DR PATRIC; fig|1379858.3.peg.164; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_0; -.
DR OrthoDB; 9782828at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000017429; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017429};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00418}.
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 160
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 44
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 202
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 43
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 106
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 294 AA; 32140 MW; AF98D63FFC4BE9C5 CRC64;
MFQGSIVALI TPFKNNEVDE KALRELVEFH IAEGTDAIVP CGTTGESATL SHEEHCHVIE
IVIEQAKKRI PVIAGAGSNS TKESVFLTEH AKKSGADAVL SITPYYNKPT QAGLYQHFKT
IAEHVDIPII LYNVPSRTGV NMLPDTVISL SKIKNIVGIK EASGSLDQAG AVLQHTDDSF
DVISGEDSLT FPMMAMGAKG VISVVANAAP KKMAQMCKAM LNNDMLLGRK LHYELLDLCK
GMFFETNPIP AKKAAYMMGL AENEIRLPLV EMTKENTQKL KSIMEKLNIK IVRD
//
