CTFB_CLOAB
ID CTFB_CLOAB Reviewed; 221 AA.
AC P23673;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acetoacetyl-CoA:acetate/butyrate CoA-transferase beta subunit {ECO:0000305};
DE EC=2.8.3.9 {ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
DE AltName: Full=Butyrate--acetoacetate CoA-transferase subunit B {ECO:0000303|PubMed:2383002};
DE Short=Coat B;
GN Name=ctfB {ECO:0000303|PubMed:8226639}; OrderedLocusNames=CA_P0164;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OG Plasmid pSOL1.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=2254264; DOI=10.1128/jb.172.12.6907-6918.1990;
RA Gerischer U., Duerre P.;
RT "Cloning, sequencing, and molecular analysis of the acetoacetate
RT decarboxylase gene region from Clostridium acetobutylicum.";
RL J. Bacteriol. 172:6907-6918(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8226639; DOI=10.1128/jb.175.21.6959-6969.1993;
RA Fischer R.J., Helms J., Duerre P.;
RT "Cloning, sequencing, and molecular analysis of the sol operon of
RT Clostridium acetobutylicum, a chromosomal locus involved in
RT solventogenesis.";
RL J. Bacteriol. 175:6959-6969(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8423010; DOI=10.1016/0378-1119(93)90545-e;
RA Petersen D.J., Cary J.W., Vanderleyden J., Bennett G.N.;
RT "Sequence and arrangement of genes encoding enzymes of the acetone-
RT production pathway of Clostridium acetobutylicum ATCC824.";
RL Gene 123:93-97(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [5]
RP PROTEIN SEQUENCE OF 1-8, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=2383002; DOI=10.1128/aem.56.6.1576-1583.1990;
RA Cary J.W., Petersen D.J., Papoutsakis E.T., Bennett G.N.;
RT "Cloning and expression of Clostridium acetobutylicum ATCC 824 acetoacetyl-
RT coenzyme A:acetate/butyrate:coenzyme A-transferase in Escherichia coli.";
RL Appl. Environ. Microbiol. 56:1576-1583(1990).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=2719476; DOI=10.1128/aem.55.2.323-329.1989;
RA Wiesenborn D.P., Rudolph F.B., Papoutsakis E.T.;
RT "Coenzyme A transferase from Clostridium acetobutylicum ATCC 824 and its
RT role in the uptake of acids.";
RL Appl. Environ. Microbiol. 55:323-329(1989).
CC -!- FUNCTION: Catalyzes the transfer of CoA from acetoacetyl-CoA to
CC acetate, butyrate and propionate (PubMed:2719476, PubMed:2383002).
CC Shows also low activity with valerate, isobutyrate and crotonate
CC (PubMed:2719476). Plays an important role in the metabolic shift
CC between the acid-producing and solvent-forming states of
CC C.acetobutylicum (PubMed:2383002). Acts mainly to detoxify the medium
CC by removing the acetate and butyrate excreted earlier in the
CC fermentation (PubMed:2719476, PubMed:2383002).
CC {ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476,
CC ECO:0000303|PubMed:2383002, ECO:0000303|PubMed:2719476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + butanoyl-CoA = acetoacetyl-CoA + butanoate;
CC Xref=Rhea:RHEA:12961, ChEBI:CHEBI:13705, ChEBI:CHEBI:17968,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57371; EC=2.8.3.9;
CC Evidence={ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12963;
CC Evidence={ECO:0000269|PubMed:2719476};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + acetyl-CoA = acetate + acetoacetyl-CoA;
CC Xref=Rhea:RHEA:27806, ChEBI:CHEBI:13705, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57288;
CC Evidence={ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27808;
CC Evidence={ECO:0000269|PubMed:2719476};
CC -!- ACTIVITY REGULATION: The acetate and butyrate conversion reactions are
CC inhibited in vitro by physiological levels of acetone and butanol.
CC {ECO:0000269|PubMed:2719476}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1200 mM for acetate {ECO:0000269|PubMed:2719476};
CC KM=660 mM for butyrate {ECO:0000269|PubMed:2719476};
CC KM=1000 mM for propionate {ECO:0000269|PubMed:2719476};
CC KM=0.021 mM for acetoacetyl-CoA (in the presence of acetate)
CC {ECO:0000269|PubMed:2719476};
CC KM=0.056 mM for acetoacetyl-CoA (in the presence of butyrate)
CC {ECO:0000269|PubMed:2719476};
CC KM=0.007 mM for acetoacetyl-CoA (in the presence of propionate)
CC {ECO:0000269|PubMed:2719476};
CC pH dependence:
CC Shows at least 80% of maximal activity from pH 5.9 to greater than
CC 7.8 for acetate conversion. {ECO:0000269|PubMed:2719476};
CC -!- SUBUNIT: Heterotetramer composed of two alpha subunits (CtfA) and two
CC beta subunits (CtfB). {ECO:0000269|PubMed:2719476}.
CC -!- INDUCTION: Transcriptionally induced or derepressed before the onset of
CC solventogenesis. {ECO:0000269|PubMed:8226639}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family.
CC {ECO:0000305}.
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DR EMBL; M55392; AAA63762.1; -; Genomic_DNA.
DR EMBL; X72831; CAA51346.1; -; Genomic_DNA.
DR EMBL; M93363; AAB53233.1; -; Genomic_DNA.
DR EMBL; AE001438; AAK76909.1; -; Genomic_DNA.
DR PIR; JN0489; JN0489.
DR RefSeq; NP_149327.1; NC_001988.2.
DR RefSeq; WP_010890848.1; NC_001988.2.
DR AlphaFoldDB; P23673; -.
DR SMR; P23673; -.
DR EnsemblBacteria; AAK76909; AAK76909; CA_P0164.
DR GeneID; 45000389; -.
DR KEGG; cac:CA_P0164; -.
DR PATRIC; fig|272562.8.peg.165; -.
DR HOGENOM; CLU_019942_4_1_9; -.
DR OMA; VAMMHTN; -.
DR OrthoDB; 1380130at2; -.
DR BioCyc; MetaCyc:COATBCLOS-MON; -.
DR SABIO-RK; P23673; -.
DR Proteomes; UP000000814; Plasmid pSOL1.
DR GO; GO:0047371; F:butyrate-acetoacetate CoA-transferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR004164; CoA_transf_AS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Plasmid; Reference proteome; Transferase.
FT CHAIN 1..221
FT /note="Acetoacetyl-CoA:acetate/butyrate CoA-transferase
FT beta subunit"
FT /id="PRO_0000157926"
FT ACT_SITE 51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ SEQUENCE 221 AA; 23624 MW; 9F9920709628F800 CRC64;
MINDKNLAKE IIAKRVAREL KNGQLVNLGV GLPTMVADYI PKNFKITFQS ENGIVGMGAS
PKINEADKDV VNAGGDYTTV LPDGTFFDSS VSFSLIRGGH VDVTVLGALQ VDEKGNIANW
IVPGKMLSGM GGAMDLVNGA KKVIIAMRHT NKGQPKILKK CTLPLTAKSQ ANLIVTELGV
IEVINDGLLL TEINKNTTID EIRSLTAADL LISNELRPMA V
