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Database: UniProt
Entry: A0A4R1NR99_9GAMM
LinkDB: A0A4R1NR99_9GAMM
Original site: A0A4R1NR99_9GAMM 
ID   A0A4R1NR99_9GAMM        Unreviewed;       301 AA.
AC   A0A4R1NR99;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:TCL07316.1};
GN   ORFNames=EZJ58_5631 {ECO:0000313|EMBL:TCL07316.1};
OS   Sodalis ligni.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=2697027 {ECO:0000313|EMBL:TCL07316.1, ECO:0000313|Proteomes:UP000294555};
RN   [1] {ECO:0000313|EMBL:TCL07316.1, ECO:0000313|Proteomes:UP000294555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=159R {ECO:0000313|EMBL:TCL07316.1,
RC   ECO:0000313|Proteomes:UP000294555};
RA   Deangelis K.;
RT   "Investigation of anaerobic lignin degradation for improved lignocellulosic
RT   biofuels.";
RL   Submitted (FEB-2019) 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:TCL07316.1}.
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DR   EMBL; SJOI01000001; TCL07316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R1NR99; -.
DR   OrthoDB; 199953at2; -.
DR   Proteomes; UP000294555; 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   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   PANTHER; PTHR12128:SF28; 2-DEHYDRO-3-DEOXY-D-GLUCONATE ALDOLASE YAGE-RELATED; 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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000294555};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         211
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   301 AA;  33334 MW;  12A8E35DABB72A75 CRC64;
     MPNPRFYGVI PPVPTLFTAD EQLDEASMAN LLDSLIASDV NGLFFLGSAG EFAHMSEALR
     FQTAEFCVNY VNKRKPVLVG IAHSGTREAI RFGLHAQKIG ADGVVAVNPY YNPLSEENLY
     LHYKHLADAL ELPILIYNFP GLTGQSIPVP IIRRLAESCE NIVGLKDTVD TLSHIRETIH
     AVKPVRPDFA VFSGYDEYLF GTLILGGDGC IPASANFAPQ LTCGIYQAWQ RQDYAEAVRL
     QQRLSFIPEL YNYDLPFYNV VKYAIQLVGV DVSVNALWPA SPLTDELKAK IKAALQRSEV
     I
//
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