ID   KCE_ACESD               Reviewed;         273 AA.
AC   E3PRK0;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=3-keto-5-aminohexanoate cleavage enzyme {ECO:0000250|UniProtKB:B0VHH0};
DE            EC=2.3.1.247 {ECO:0000250|UniProtKB:B0VHH0};
GN   Name=kce {ECO:0000250|UniProtKB:B0VHH0}; OrderedLocusNames=CLOST_1384;
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
CC   -!- FUNCTION: Involved in the anaerobic fermentation of lysine. Catalyzes
CC       the reversible reaction between 3-keto-5-aminohexanoate (KAH) and
CC       acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction
CC       involves the deprotonation of KAH, the nucleophilic addition onto
CC       acetyl-CoA and the intramolecular transfer of the CoA moiety.
CC       {ECO:0000250|UniProtKB:B0VHH0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3-
CC         aminobutanoyl-CoA + acetoacetate; Xref=Rhea:RHEA:31555,
CC         ChEBI:CHEBI:13705, ChEBI:CHEBI:57288, ChEBI:CHEBI:57366,
CC         ChEBI:CHEBI:58523; EC=2.3.1.247;
CC         Evidence={ECO:0000250|UniProtKB:B0VHH0};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC       pathway. {ECO:0000250|UniProtKB:B0VHH0}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:B0VHH0}.
CC   -!- SIMILARITY: Belongs to the KCE family. {ECO:0000305}.
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DR   EMBL; FP565809; CBH21504.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PRK0; -.
DR   SMR; E3PRK0; -.
DR   STRING; 1511.CLOST_1384; -.
DR   EnsemblBacteria; CBH21504; CBH21504; CLOST_1384.
DR   KEGG; cst:CLOST_1384; -.
DR   eggNOG; COG3246; Bacteria.
DR   HOGENOM; CLU_065536_2_0_9; -.
DR   OMA; LWIGPGQ; -.
DR   UniPathway; UPA00870; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0043720; F:3-keto-5-aminohexanoate cleavage activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR008567; KCE_family.
DR   PANTHER; PTHR37418; PTHR37418; 1.
DR   Pfam; PF05853; BKACE; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..273
FT                   /note="3-keto-5-aminohexanoate cleavage enzyme"
FT                   /id="PRO_0000416976"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         82..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         106..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B0VHH0"
SQ   SEQUENCE   273 AA;  29685 MW;  F52ED6437317FD2F CRC64;
     MEKLIITAAI CGAEVTKEHN PNVPYTVEEI VREAKSAYDA GASVIHLHVR EDDGTPTQSK
     ERFKMCVDAI KEACPDAIIQ PSTGGAVGMT DEERLQPVFL KPEMASLDCG TCNFGGDEIF
     VNTENMIINF SKYMIKNGVK PECEVFDKSM IDMAIRLAKK GHIQTPMHFN FVMGVNGGIS
     ATPRDLVFLI GSIPSESSFT VSAMGRNQFP MAAMAIITGG HVRVGFEDNV YIEKGVPAKS
     NGELVEKVVR LAKEFGRPVA TPSEAREILG ISK