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Database: UniProt
Entry: A0A920C9X8_9BACL
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ID   A0A920C9X8_9BACL        Unreviewed;       297 AA.
AC   A0A920C9X8;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   05-FEB-2025, entry version 9.
DE   SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:GIO29589.1};
GN   Name=dapA_1 {ECO:0000313|EMBL:GIO29589.1};
GN   ORFNames=J2TS6_07300 {ECO:0000313|EMBL:GIO29589.1};
OS   Paenibacillus albilobatus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=2716884 {ECO:0000313|EMBL:GIO29589.1, ECO:0000313|Proteomes:UP000679779};
RN   [1] {ECO:0000313|EMBL:GIO29589.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J2TS6 {ECO:0000313|EMBL:GIO29589.1};
RA   Okamoto M., Kumagai M., Kanamori H., Takamatsu D.;
RT   "Antimicrobial resistance genes in bacteria isolated from Japanese honey,
RT   and their potential for conferring macrolide and lincosamide resistance in
RT   the American foulbrood pathogen Paenibacillus larvae.";
RL   Submitted (MAR-2021) 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:GIO29589.1}.
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DR   EMBL; BORQ01000001; GIO29589.1; -; Genomic_DNA.
DR   Proteomes; UP000679779; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128:SF72; 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:UP000679779}.
FT   ACT_SITE        134
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        162
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         202
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   297 AA;  32831 MW;  9BE6B1A2239E3C08 CRC64;
     MSKFPGIYVA TVTPFTASYE VDFNRLKEHV DWLIQKGVDG IIPTGSLGEY ATLTSEERAQ
     VITATIDAAA GRVPVVIGGA APSTKQVVEL IQFSKEKGAE GVMALPPINY KPTEDEVVAH
     YEAVSNAGLP VIVYNNPYDY PVDLTPRILQ KLSKFENIVA VKEFSGDVRR VYDILRETDL
     EVMIGVDDLA LEGALAGATG WIAGFANAFP RESITVFNMT RTGRVDEALE LYRYLLPLFH
     FDANPRLVQA IKYVMDFVGQ PAGPSRPPRL PLPEEDRLAV QEAYKYAVNR PIRIVQE
//
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