ID A0A077PGM4_XENBV Unreviewed; 297 AA.
AC A0A077PGM4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=XBKQ1_1650005 {ECO:0000313|EMBL:CDH18894.1};
OS Xenorhabdus bovienii str. kraussei Quebec.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1398203 {ECO:0000313|EMBL:CDH18894.1, ECO:0000313|Proteomes:UP000028500};
RN [1] {ECO:0000313|EMBL:CDH18894.1, ECO:0000313|Proteomes:UP000028500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kraussei Quebec {ECO:0000313|Proteomes:UP000028500};
RA Murfin K., Klassen J., Lee M., Forst S., Stock P., Goodrich-Blair H.;
RT "Sub-species coevolution in mutualistic symbiosis.";
RL Submitted (JUL-2013) 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:CDH18894.1}.
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DR EMBL; CBSY010000074; CDH18894.1; -; Genomic_DNA.
DR RefSeq; WP_038246459.1; NZ_HG427643.1.
DR AlphaFoldDB; A0A077PGM4; -.
DR HOGENOM; CLU_049343_5_0_6; -.
DR OrthoDB; 199953at2; -.
DR Proteomes; UP000028500; 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:UP000028500}.
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 159
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 44
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 297 AA; 31691 MW; E96D687C41D0E37C CRC64;
MFSGLSAFPL TPTNENGIDE AAFVRLIERL VVANVDSIGA LGSTGNYAYF TLAERLRVTQ
LAVQHAGNTP VIIGIGALRT RDVLDLAEGA QTAGASAVLL APISYQRLSA DEVFGLYETV
TRNLSVPLCV YDNPNMTHFE FSDELHGRIA HLPNVCSIKI PGVTVDPVAA KARVERLRAL
IPSHVTIGIS GDGFAATGLN AGCEVWYSVI GGLFPKAALA ITRAAQAGDI QEVTRLSERL
QPLWTFFRQY GGSLRVVASA AVLLGLVEQD CLPLPLKALE AADLQQLAEL LDELELA
//
