ID D7N7S3_9FIRM Unreviewed; 447 AA.
AC D7N7S3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=HMPREF0629_00114 {ECO:0000313|EMBL:EFI41492.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41492.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI41492.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI41492.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-2010) 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}.
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DR EMBL; GL349422; EFI41492.1; -; Genomic_DNA.
DR RefSeq; WP_009221431.1; NZ_GL349422.1.
DR AlphaFoldDB; D7N7S3; -.
DR STRING; 575609.HMPREF0629_00114; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
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:UP000004712};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03227, ECO:0000313|EMBL:EFI41492.1}.
FT DOMAIN 7..184
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; 49209 MW; 8BABF1C953D1F32F CRC64;
MDCKNIYKDK LISAAKAASF VKSGDYVDYA WGAQTPVAID RELAKRAGEL KDVVVRGGVL
LWTPEIFKAD PNGDSFIWYS WHSGGADRVR INTTDAGFYA PIRYSEVPRY YRENCKVDVA
YITVTPMDEH GYFNMGLNAS HMMAICETAK IVIVEVNEKL PVALGGFENT IHVSEVDYIV
EGDNPEMAEL PAGAFGDVDR KVAEIIVNEI PNGACIQLGI GGMPNAVGSL IAESDLKDLG
VHTEMFVDAF VDLYNKGKIT GAKKNIDRFR QTYAFAAGTK KLYDFIDNNP QCMAAPVDYT
NDARVISKID NFVSINNAVN VDLVGQVSSE SSGKKHISGA GGQLDFVLGA YLSNGGKSFI
CLSSKFYNKK TGKEESRIVP NFETGSAITV ARPNTHYIVT EYGLFNCKGK SNWERAEGII
NLAAPEFRDD LIKEAEKFGI WRNSNRR
//
