ID A0A1I2AJF7_9FIRM Unreviewed; 452 AA.
AC A0A1I2AJF7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Probable butyrate:acetyl-CoA coenzyme A-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE Short=Butyrate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE EC=2.8.3.- {ECO:0000256|HAMAP-Rule:MF_03228};
GN ORFNames=SAMN02910327_01204 {ECO:0000313|EMBL:SFE43909.1};
OS Peptostreptococcaceae bacterium pGA-8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=1520829 {ECO:0000313|EMBL:SFE43909.1, ECO:0000313|Proteomes:UP000242361};
RN [1] {ECO:0000313|Proteomes:UP000242361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=pGA-8 {ECO:0000313|Proteomes:UP000242361};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Coenzyme A-transferase that converts butyrate to butyryl-CoA.
CC {ECO:0000256|HAMAP-Rule:MF_03228}.
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_03228};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_03228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632, ECO:0000256|HAMAP-Rule:MF_03228}.
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DR EMBL; FONK01000009; SFE43909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2AJF7; -.
DR STRING; 1520829.SAMN02910327_01204; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000242361; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0019605; P:butyrate metabolic 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_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 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW Hydrolase {ECO:0000313|EMBL:SFE43909.1};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW Reference proteome {ECO:0000313|Proteomes:UP000242361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03228}.
FT DOMAIN 11..190
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 282..435
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 249
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 224..228
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 323
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 346
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
SQ SEQUENCE 452 AA; 49781 MW; A792ED3F07122CF9 CRC64;
MYRLDEIFKI YQEKLITADE AAAMVEPNNR IHFGLGLGVV KDLDAALARR ADTLRGVEVV
STVGIQQDFL HLYKAGQSLD NVRFASAHYN GFDRKMAVND KCWYIPMNFN ELPSYWDQND
CQVDIAMLQV GPMDKYGNFN LGPQVSDIWG VLKSAKMVIV EVNTKMPRTH GVENTINLAD
IDFVVEGSNT EMAQIPPGKA SEIDKKIASF VVEKIRDNST LQLGIGALPS TIGTLLAESD
VKDISGHTEM LVDGYLELYK AGKLTNKKAV NPGKLVYAFA GGSQDLYDFI DDNPICHVAP
VDYVNNQGVI ASMDNFVSVN SCIKVDLFGQ ICSETSNHMH ISGTGGQLDF VQGAYHSKGG
QSFICTPSTR KFPDGKVRSL ILPSMIAGYV VTTPRTCTHW VVTEFGAVNL KGKSTWQRAE
ALISIAHPDF QEYLIGMAEK IGIWRTTSKC TL
//
