ID C4ILY9_CLOBU Unreviewed; 309 AA.
AC C4ILY9;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Dihydrodipicolinate synthetase family protein {ECO:0000313|EMBL:EEP52788.1};
GN ORFNames=CLP_0167 {ECO:0000313|EMBL:EEP52788.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP52788.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP52788.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) 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:EEP52788.1}.
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DR EMBL; ACOM01000007; EEP52788.1; -; Genomic_DNA.
DR RefSeq; WP_003410324.1; NZ_ACOM01000007.1.
DR AlphaFoldDB; C4ILY9; -.
DR STRING; 1492.ATN24_15415; -.
DR GeneID; 66380537; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_9; -.
DR Proteomes; UP000003081; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
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.
DR PROSITE; PS00665; DHDPS_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000003081}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 52
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 208
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 309 AA; 34410 MW; DA74A29BC316C0CF CRC64;
MSKFDIKAFK GVIPAVLTVF DKEENIDEVG MRQLVSFLID KGVNGLYLTG STGEGFTMTS
EERKKVVEIV IDETAGRVPV VVHVGAIGTK ISIDLAKHAE SVGADGISSV PPFYWKFNEN
QIIKYYEDIA NSCSIPMIVY NVPLVGLLGM NAIKRLAKIE NVKGIKYTAL SQYEITQIKD
EVGEEFLVYS GADEMAMSGL IAGADGIVGS FYNIMPELFI NIYDAVKNKD LDEAQRLQKQ
AVEVIMYALQ LPSFYAGMKV ILKWMGINAG YCRRPFENLT EEDEVKFKEG FKKLKETYDL
KGIDFIDAI
//
