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Database: UniProt
Entry: A0A0S2W0K4_9FIRM
LinkDB: A0A0S2W0K4_9FIRM
Original site: A0A0S2W0K4_9FIRM 
ID   A0A0S2W0K4_9FIRM        Unreviewed;       307 AA.
AC   A0A0S2W0K4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=IB211_00457 {ECO:0000313|EMBL:ALP92852.1};
OS   Intestinimonas butyriciproducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX   NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP92852.1, ECO:0000313|Proteomes:UP000064844};
RN   [1] {ECO:0000313|EMBL:ALP92852.1, ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|EMBL:ALP92852.1,
RC   ECO:0000313|Proteomes:UP000064844};
RX   PubMed=26620920; DOI=10.1038/ncomms10062;
RA   Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT   "Production of butyrate from lysine and the Amadori product fructoselysine
RT   by a human gut commensal.";
RL   Nat. Commun. 6:10062-10062(2015).
RN   [2] {ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA   de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT   "A butyrogenic pathway from the amino acid lysine in a human gut
RT   commensal.";
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, 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; CP011307; ALP92852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2W0K4; -.
DR   STRING; 1297617.IB211_00457; -.
DR   KEGG; ibu:IB211_00457; -.
DR   PATRIC; fig|1297617.4.peg.462; -.
DR   eggNOG; COG0329; Bacteria.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000064844; 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; IPR020624; Schiff_base-form_aldolases_CS.
DR   NCBIfam; TIGR00674; dapA; 1.
DR   PANTHER; PTHR12128:SF15; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00418}; Cytoplasm {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:UP000064844};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00418}.
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT                   ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         52
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         214
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            51
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT   SITE            114
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   307 AA;  33379 MW;  77587BC1E72C8100 CRC64;
     MNQFVEKYGQ ILLPLITPYD ANEEVDYGKY AELIEYLIQN DLCDSLIVTG TTGEASLLTF
     DERVKLMETA VKTAAGRKPV IAGTGCASTK ETIALTNKAV DLGIETCLVV CPFYNKPTQE
     GLYRHFKALA EATKADIMLY NIPIFVGVNL EAETVRRLAA LPNIVGVKDE AGINPTQVTD
     FFLATQDVDP DFAIYNGDDV MLLPTIVQGA MGLVSGGAHI FGHEIRAIFK AFAEGDNQRA
     KELFVPIYRF CKSTGQNGRI LPNSILRPAI ELVTGIHLGP ARSPLAPATE EETAVTTAIL
     REIGKLN
//
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