ID A0A161YRM4_9CLOT Unreviewed; 297 AA.
AC A0A161YRM4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative 2-keto-3-deoxy-galactonate aldolase YagE {ECO:0000313|EMBL:KZL93632.1};
DE EC=4.1.2.- {ECO:0000313|EMBL:KZL93632.1};
GN Name=yagE_1 {ECO:0000313|EMBL:KZL93632.1};
GN ORFNames=CLMAG_06780 {ECO:0000313|EMBL:KZL93632.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL93632.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL93632.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL93632.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) 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:KZL93632.1}.
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DR EMBL; LWAE01000001; KZL93632.1; -; Genomic_DNA.
DR RefSeq; WP_066617889.1; NZ_LWAE01000001.1.
DR AlphaFoldDB; A0A161YRM4; -.
DR STRING; 1121326.CLMAG_06780; -.
DR PATRIC; fig|1121326.3.peg.637; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000076603; 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; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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:UP000076603}.
FT ACT_SITE 133
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 45
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 209
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 297 AA; 33105 MW; 118CFA1238421449 CRC64;
MFRGVFTPMV TIFDENGNFD KESNRFMIEK LISDGIYGIC LLGTTGEFFN MSFEEKAEYI
KFASETINGR VKLIVGAGSN NIKEAIALTK CAEENNADAI LALPPFYFKL DDNHVYEYFA
AIAKNTKLPI VLYNIPNNTN VSLSADLILK LANNFENIAN GGVKDTTPAL SNVRNFVERV
KKVHKNFSVY SGIDEYLIPN LMIGGDGIIG TQTNTQAKLL VDTFKAFDAK DFDKLLSNQQ
EINRIMAVRE MPGNNILSTK TAVSIALGLD FNTSLRYYNI TSDENTKERI KNVVKPS
//
