ID A0A448V2X4_9FIRM Unreviewed; 446 AA.
AC A0A448V2X4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=scpC {ECO:0000313|EMBL:VEJ36127.1};
GN ORFNames=NCTC13079_01324 {ECO:0000313|EMBL:VEJ36127.1};
OS Peptoniphilus ivorii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=54006 {ECO:0000313|EMBL:VEJ36127.1, ECO:0000313|Proteomes:UP000269544};
RN [1] {ECO:0000313|EMBL:VEJ36127.1, ECO:0000313|Proteomes:UP000269544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13079 {ECO:0000313|EMBL:VEJ36127.1,
RC ECO:0000313|Proteomes:UP000269544};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LR134523; VEJ36127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448V2X4; -.
DR KEGG; piv:NCTC13079_01324; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000269544; Chromosome 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:UP000269544};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03227, ECO:0000313|EMBL:VEJ36127.1}.
FT DOMAIN 3..189
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 278..434
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 446 AA; 48821 MW; 4CA3CECCF6D01A91 CRC64;
MDYKKLYDQK LITAKEAAAK IKSGDWVEYG WGAGTSTAVD AELAKRMDEL EDVKLRGGVT
FKAPQVLSAD PEGKHFIWNS WHAGGPERKA VNAGPGAFYN PLRYSELPKY YRDEVELDVA
IVTTTPMDKH GYFNFGLNAS HTMAGIEKAK MVIVEVNEAM PYCPGKCESE VHIDRVDFIV
EAGNVPLAEV PKGSYGEVDE KVAEFIVNEI PDGATLQLGI GGMPNAVGAL IADSDLKDLG
VHSEMYVDAF VDMAKKGKVN GSKKTIDKYR QVYAFAAGSA ELYEYLDHNP ECMAAPVNYT
NGAEVVKEID NFISINNALN VDLWGQVSSE STGLRHISGA GGQLDFALGA YLSKGGKSFI
CLSSTFTNKK GETVSRILPN FATGSAITVA RPNTHYIVTE YGIFNCKGRT TWERAEGLIE
LAHPDFRDEL IKNAEEMGIW RASNKR
//