ID A0A0M2LLG0_9MICO Unreviewed; 301 AA.
AC A0A0M2LLG0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:KKI16262.1};
GN ORFNames=XM48_15645 {ECO:0000313|EMBL:KKI16262.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI16262.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI16262.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI16262.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKI16262.1}.
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DR EMBL; LAYO01000111; KKI16262.1; -; Genomic_DNA.
DR RefSeq; WP_046456782.1; NZ_LAYO01000111.1.
DR AlphaFoldDB; A0A0M2LLG0; -.
DR STRING; 1642040.XM48_15645; -.
DR PATRIC; fig|1642040.3.peg.927; -.
DR OrthoDB; 9778880at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; 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; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 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:UP000033836}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 168
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 301 AA; 31572 MW; E962DC686A883DF7 CRC64;
MTRKNANLGG VLAAIPTPFT TDGAAVDADG IRAQIDRMVA GGVAGVVPTG TSGEFTSLTP
EEYREVIRLN VEAAAGRIKV VAGIGHTSTT GAIDLARYAE EVGADAVMVV PPFYDPLSFD
ALKAFLRAVA DSIELQIMYY NVPGATGVTL DAEQLAEIGD IDGVDYFKDT SGDAVSLTDV
LTSRTDRITA FNGWDTLTFL GITLGAKGSV WGVASVAPAQ AAELFRVIAE EKDLDRGREL
WAPLWNLSSV LESVNYPAGL KAALELLGTP VGPVREPILP LADADRERIA EALRGVGVLA
A
//
