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Database: UniProt
Entry: A0A2P8CXR2_9BACT
LinkDB: A0A2P8CXR2_9BACT
Original site: A0A2P8CXR2_9BACT 
ID   A0A2P8CXR2_9BACT        Unreviewed;       293 AA.
AC   A0A2P8CXR2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:PSK89761.1};
GN   ORFNames=B0I18_11060 {ECO:0000313|EMBL:PSK89761.1};
OS   Taibaiella chishuiensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Taibaiella.
OX   NCBI_TaxID=1434707 {ECO:0000313|EMBL:PSK89761.1, ECO:0000313|Proteomes:UP000240572};
RN   [1] {ECO:0000313|EMBL:PSK89761.1, ECO:0000313|Proteomes:UP000240572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12700 {ECO:0000313|EMBL:PSK89761.1,
RC   ECO:0000313|Proteomes:UP000240572};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {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:PSK89761.1}.
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DR   EMBL; PYGD01000010; PSK89761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8CXR2; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000240572; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128:SF73; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240572}.
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         49
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   293 AA;  31903 MW;  B3EA36C4A4C954B8 CRC64;
     MNRIPFEGVI AYPITPFDDQ DRVDLPLFRS LLERLVISGA NGIAPLGSTG VLPYLRREEE
     EALTEATLQQ VDGRLPVLVG VSHLTTADTI YHARFAEKAG AAAVMILPMS YWKLSDEEIF
     RHYESVAQAI NIPIMAYNNP ATSGLDMSPA LLRRLLGIDN VTMIKESSGD IHRMHLLQQM
     LGDDAALYNG SNPMALAAFA AGARGWCTAA PNLVPEQNNA LYQAIRQNDL ARAQASFTQQ
     AGLLRFMVAK GLPRVVQAGL ELRGIPSGGL RKPLLPLSAD EKNTLQELLK ACS
//
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