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Database: UniProt
Entry: A0A448V2X4_9FIRM
LinkDB: A0A448V2X4_9FIRM
Original site: A0A448V2X4_9FIRM 
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}.
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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
//
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