ID A0A084ZQA5_9ENTR Unreviewed; 297 AA.
AC A0A084ZQA5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:KFB99649.1};
DE EC=4.-.-.- {ECO:0000313|EMBL:KFB99649.1};
GN ORFNames=GTGU_04088 {ECO:0000313|EMBL:KFB99649.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFB99649.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFB99649.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFB99649.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFB99649.1}.
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DR EMBL; JMTB01000114; KFB99649.1; -; Genomic_DNA.
DR RefSeq; WP_038161529.1; NZ_JMTB01000114.1.
DR AlphaFoldDB; A0A084ZQA5; -.
DR eggNOG; COG0329; Bacteria.
DR OrthoDB; 199953at2; -.
DR Proteomes; UP000028630; 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 Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 136
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 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 297 AA; 32654 MW; B25BC023299D3845 CRC64;
MTTHSRFSGV WCPSITPMDA QGALDMNGLS QHLARLTAAR IDVILLMGSI GEFASLSLVE
RLKLIREARA MSPLAMVANV SSTCVADIVR MAEEAFRTGY DGVMVLPPYY YGQTANQLLS
YFRALGKQFS GKWFAYNFPA RTGCDITPEI TATLAKEFPN FAGIKDTVDC QSHTRNIILA
TEAVRNDFAV LSGYDEYFIP NLLAGGAGII SGLNNIMPEL FVQAREAWAA GDFQTLHNVQ
REIGRFMSIY SIGDDFVTTI KTVVSRKFGY CQPHSRNFGG ELSAAQCQHI DSVFGIQ
//
