KCE_CLOAI
ID KCE_CLOAI Reviewed; 276 AA.
AC B0VHH0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=3-keto-5-aminohexanoate cleavage enzyme {ECO:0000303|PubMed:21632536};
DE EC=2.3.1.247 {ECO:0000269|PubMed:21632536};
GN Name=kce {ECO:0000303|PubMed:21632536}; OrderedLocusNames=CLOAM0912;
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas.
OX NCBI_TaxID=459349;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry;
RX PubMed=18245282; DOI=10.1128/jb.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 2-276 IN COMPLEXES WITH
RP 5-AMINO-3-OXO-HEXANOATE AND ACETOACETATE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, MUTAGENESIS OF SER-82; GLU-143;
RP ARG-226 AND ASP-231, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=21632536; DOI=10.1074/jbc.m111.253260;
RA Bellinzoni M., Bastard K., Perret A., Zaparucha A., Perchat N., Vergne C.,
RA Wagner T., de Melo-Minardi R.C., Artiguenave F., Cohen G.N.,
RA Weissenbach J., Salanoubat M., Alzari P.M.;
RT "3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon
RT Claisen-type condensation.";
RL J. Biol. Chem. 286:27399-27405(2011).
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:0000269|PubMed:21632536}.
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:0000269|PubMed:21632536};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21632536};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.208 mM for KAH {ECO:0000269|PubMed:21632536};
CC KM=0.012 mM for acetoacetate {ECO:0000269|PubMed:21632536};
CC Note=kcat is 2.69 sec(-1) for 3-keto-5-aminohexanoate cleavage.
CC {ECO:0000269|PubMed:21632536};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000305|PubMed:21632536}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21632536}.
CC -!- SIMILARITY: Belongs to the KCE family. {ECO:0000305}.
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DR EMBL; CU466930; CAO80785.1; -; Genomic_DNA.
DR RefSeq; WP_015424643.1; NC_020449.1.
DR PDB; 2Y7D; X-ray; 1.59 A; A/B/C/D=2-276.
DR PDB; 2Y7E; X-ray; 1.28 A; A/B=2-276.
DR PDB; 2Y7F; X-ray; 1.75 A; A/B/C/D=2-276.
DR PDB; 2Y7G; X-ray; 1.40 A; A/B=2-276.
DR PDBsum; 2Y7D; -.
DR PDBsum; 2Y7E; -.
DR PDBsum; 2Y7F; -.
DR PDBsum; 2Y7G; -.
DR AlphaFoldDB; B0VHH0; -.
DR SMR; B0VHH0; -.
DR STRING; 459349.CLOAM0912; -.
DR EnsemblBacteria; CAO80785; CAO80785; CLOAM0912.
DR KEGG; caci:CLOAM0912; -.
DR eggNOG; COG3246; Bacteria.
DR HOGENOM; CLU_065536_2_0_0; -.
DR OMA; VPEYEIF; -.
DR OrthoDB; 1892901at2; -.
DR BRENDA; 2.3.1.247; 14207.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002019; 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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..276
FT /note="3-keto-5-aminohexanoate cleavage enzyme"
FT /id="PRO_0000416975"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21632536"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21632536"
FT MUTAGEN 82
FT /note="S->G: Reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:21632536"
FT MUTAGEN 143
FT /note="E->G,Q: Reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:21632536"
FT MUTAGEN 226
FT /note="R->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21632536"
FT MUTAGEN 231
FT /note="D->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21632536"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:2Y7E"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2Y7E"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2Y7E"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2Y7E"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 244..258
FT /evidence="ECO:0007829|PDB:2Y7E"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:2Y7E"
SQ SEQUENCE 276 AA; 30222 MW; 524B0E27FFC0FA5D CRC64;
MEPLILTAAI TGAETTRADQ PNLPITPEEQ AKEAKACFEA GARVIHLHIR EDDGRPSQRL
DRFQEAISAI REVVPEIIIQ ISTGGAVGES FDKRLAPLAL KPEMATLNAG TLNFGDDIFI
NHPADIIRLA EAFKQYNVVP EVEVYESGMV DAVARLIKKG IITQNPLHIQ FVLGVPGGMS
GKPKNLMYMM EHLKEEIPTA TWAVAGIGRW HIPTSLIAMV TGGHIRCGFE DNIFYHKGVI
AESNAQLVAR LARIAKEIGR PLATPEQARE ILALNK
