KCE_FUSNN
ID KCE_FUSNN Reviewed; 272 AA.
AC Q8RHX2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=3-keto-5-aminohexanoate cleavage enzyme {ECO:0000303|PubMed:6811551};
DE EC=2.3.1.247 {ECO:0000269|PubMed:6811551};
GN Name=kce {ECO:0000303|PubMed:17166837}; OrderedLocusNames=FN1868;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:6811551};
RX PubMed=6811551; DOI=10.1128/jb.152.1.201-207.1982;
RA Barker H.A., Kahn J.M., Hedrick L.;
RT "Pathway of lysine degradation in Fusobacterium nucleatum.";
RL J. Bacteriol. 152:201-207(1982).
RN [3]
RP FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:17166837};
RX PubMed=17166837; DOI=10.1074/jbc.m609829200;
RA Kreimeyer A., Perret A., Lechaplais C., Vallenet D., Medigue C.,
RA Salanoubat M., Weissenbach J.;
RT "Identification of the last unknown genes in the fermentation pathway of
RT lysine.";
RL J. Biol. Chem. 282:7191-7197(2007).
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. It can
CC also use beta-alanyl-CoA as substrate. {ECO:0000269|PubMed:17166837,
CC ECO:0000269|PubMed:6811551}.
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:6811551};
CC -!- ACTIVITY REGULATION: 3-fold increase in activity by addition of 10 mM
CC 2-mercaptoethanol. Addition of CoCl(2) and to a lesser extent MnCl(2)
CC increase the activity but not MgCl(2). Inhibited by phosphate buffers
CC but not by 5,5'-dithio-2-nitrobenzoic acid.
CC {ECO:0000269|PubMed:6811551}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.0. The half-maximal rate is observed at 5.2 and
CC 8.1. {ECO:0000269|PubMed:6811551};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000269|PubMed:6811551, ECO:0000305|PubMed:17166837}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17166837}.
CC -!- SIMILARITY: Belongs to the KCE family. {ECO:0000305}.
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DR EMBL; AE009951; AAL93967.1; -; Genomic_DNA.
DR RefSeq; NP_602668.1; NC_003454.1.
DR AlphaFoldDB; Q8RHX2; -.
DR SMR; Q8RHX2; -.
DR STRING; 190304.FN1868; -.
DR EnsemblBacteria; AAL93967; AAL93967; FN1868.
DR KEGG; fnu:FN1868; -.
DR PATRIC; fig|190304.8.peg.344; -.
DR eggNOG; COG3246; Bacteria.
DR HOGENOM; CLU_065536_2_0_0; -.
DR InParanoid; Q8RHX2; -.
DR OMA; VPEYEIF; -.
DR BioCyc; FNUC190304:G1FZS-365-MON; -.
DR BioCyc; MetaCyc:MON-12289; -.
DR BRENDA; 2.3.1.247; 11865.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002521; 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 Metal-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..272
FT /note="3-keto-5-aminohexanoate cleavage enzyme"
FT /id="PRO_0000416977"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 83..86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B0VHH0"
SQ SEQUENCE 272 AA; 30137 MW; 01A15D738B169915 CRC64;
MMEKLIITAA ICGAEVTKEH NPAVPYTVEE IAREAESAYK AGASIIHLHV REDDGTPTQD
KERFRKCIEA IREKCPDVII QPSTGGAVGM TDLERLQPTE LHPEMATLDC GTCNFGGDEI
FVNTENTIKN FGKILIERGV KPEIEVFDKG MIDYAIRYQK QGFIQKPMHF DFVLGVQMSA
SARDLVFMSE SIPEGSTWTV AGVGRHQFQM AALAIVMGGH VRVGFEDNVY IDKGILAKSN
GELVERVVRL AKELGREIAT PDEARQILSL KK
