ID G4D6L4_9FIRM Unreviewed; 447 AA.
AC G4D6L4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Butyryl-CoA:acetate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03227};
DE Short=Butyryl-CoA CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03227};
DE EC=2.8.3.- {ECO:0000256|HAMAP-Rule:MF_03227};
GN Name=cat {ECO:0000313|EMBL:EGY76466.1};
GN ORFNames=HMPREF9129_2044 {ECO:0000313|EMBL:EGY76466.1};
OS Peptoniphilus indolicus ATCC 29427.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY76466.1, ECO:0000313|Proteomes:UP000003422};
RN [1] {ECO:0000313|EMBL:EGY76466.1, ECO:0000313|Proteomes:UP000003422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY76466.1,
RC ECO:0000313|Proteomes:UP000003422};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Coenzyme A-transferase that converts butyryl-CoA to butyrate.
CC {ECO:0000256|HAMAP-Rule:MF_03227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + butanoate = acetate + butanoyl-CoA;
CC Xref=Rhea:RHEA:30071, ChEBI:CHEBI:17968, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57371; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03227};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_03227}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC Butyryl-CoA CoA-transferase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03227}.
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:EGY76466.1}.
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DR EMBL; AGBB01000208; EGY76466.1; -; Genomic_DNA.
DR RefSeq; WP_004822990.1; NZ_JH165067.1.
DR AlphaFoldDB; G4D6L4; -.
DR STRING; 997350.HMPREF9129_2044; -.
DR PATRIC; fig|997350.3.peg.1951; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000003422; Unassembled WGS sequence.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046358; P:butyrate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR HAMAP; MF_03227; But_acet_CoA_trans; 1.
DR HAMAP; MF_03228; But_CoA_trans; 1.
DR InterPro; IPR026888; AcetylCoA_hyd_C.
DR InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR InterPro; IPR046433; ActCoA_hydro.
DR InterPro; IPR003702; ActCoA_hydro_N.
DR InterPro; IPR023990; Butryl-CoA_acetate_CoA_Tfrase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR03948; butyr_acet_CoA; 1.
DR PANTHER; PTHR21432:SF20; ACETYL-COA HYDROLASE; 1.
DR PANTHER; PTHR21432; ACETYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_03227};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03227};
KW Reference proteome {ECO:0000313|Proteomes:UP000003422};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03227, ECO:0000313|EMBL:EGY76466.1}.
FT DOMAIN 4..182
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 278..435
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 244
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 219..223
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 319
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 342
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
SQ SEQUENCE 447 AA; 48850 MW; A0D95F7317A6C1B2 CRC64;
MDFKKEYQDK LISAEKAASF VKSGDTIDFA WAAQTPVAID KALAKRAGEL ENVVVMGGVL
MGVPEIFNAD PEGNAFIWKT WHAGGADRNR INKTDAGFYA PLRYSELPRW YRENIDLNIA
YLATTPMDKH GYFNFGLNAS HLKAAIEVAD LVVVEVNENL PVALGGVENV VHISEVDYIV
EGENPDIKEL PAGSFGDVDK KVAELIVGEM VDGSCIQLGI GGMPNAVGSL LAQSDLKDLG
VHTEMLVDAF VDLANAGKIT GARKNIDRYR QTYAFAAGTK KLYDFVDNNP SCMASTVGYT
NDARVIAQLD NFVSINNAVN VDLFGQVSSE SSGFRHISGA GGQLDFVLGA YLSKGGKSFI
CLSSKFYNKK EDKEESRIVL NFEPGTIITA ARPNTHYIVT EHGIFNCKGK STWERAEGII
NLASPEFRED LIKQAEKAGI WRKSNRK
//
