ID A0A916T228_9SPHN Unreviewed; 304 AA.
AC A0A916T228;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 08-OCT-2025, entry version 10.
DE SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:GGB26739.1};
GN ORFNames=GCM10011380_15400 {ECO:0000313|EMBL:GGB26739.1};
OS Sphingomonas metalli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1779358 {ECO:0000313|EMBL:GGB26739.1, ECO:0000313|Proteomes:UP000623067};
RN [1] {ECO:0000313|EMBL:GGB26739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15330 {ECO:0000313|EMBL:GGB26739.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGB26739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15330 {ECO:0000313|EMBL:GGB26739.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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:GGB26739.1}.
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DR EMBL; BMIH01000002; GGB26739.1; -; Genomic_DNA.
DR RefSeq; WP_188658164.1; NZ_BMIH01000002.1.
DR Proteomes; UP000623067; 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:UP000623067}.
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 206
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 304 AA; 33275 MW; AE9045CEB5A1FB91 CRC64;
MSIDWQGVFP AVTTQIREDL SIDLADTQRV VDDLIRDGVT GVIALGTVGE NNSLTFEEKI
EVLTAIVEAV DKRVPVVTGV SEYDTRRAVG YAQAAEKAGA DGLMLLPPMV YVPKAKELAA
HFRGVAEKTA LPIMLYNNPP AYRTQINNEV LGLVADVANI VAIKESAPDT RRFSDVKNRF
GDRFVLFAGL DDVALEGLYL GAQGWVSGLT NAFPKESVEL VNAFKRGDHG KAMEIYRWFM
PLLHLDAEHD LVQSIKLAEQ VMGRGSERVL PPRYVLEGER RAEVIAMVEQ AAATRPTLTL
AKAA
//
