ID C7HSG8_9FIRM Unreviewed; 445 AA.
AC C7HSG8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=abfT {ECO:0000313|EMBL:EEU13084.1};
GN ORFNames=HMPREF0078_0217 {ECO:0000313|EMBL:EEU13084.1};
OS Anaerococcus vaginalis ATCC 51170.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=655811 {ECO:0000313|EMBL:EEU13084.1, ECO:0000313|Proteomes:UP000003821};
RN [1] {ECO:0000313|EMBL:EEU13084.1, ECO:0000313|Proteomes:UP000003821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51170 {ECO:0000313|EMBL:EEU13084.1,
RC ECO:0000313|Proteomes:UP000003821};
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., Gibbs R.;
RL Submitted (AUG-2009) 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}.
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:EEU13084.1}.
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DR EMBL; ACXU01000005; EEU13084.1; -; Genomic_DNA.
DR RefSeq; WP_004838193.1; NZ_GG700527.1.
DR AlphaFoldDB; C7HSG8; -.
DR GeneID; 79021504; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000003821; 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: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 Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW Reference proteome {ECO:0000313|Proteomes:UP000003821};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03228, ECO:0000313|EMBL:EEU13084.1}.
FT DOMAIN 4..182
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_03228"
FT BINDING 219..223
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 319
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 342
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
SQ SEQUENCE 445 AA; 49176 MW; 9ACC8C4386E07CB2 CRC64;
MDYNKLYKEK LISAEDAAKL VKDGDYVDYS WGIISPHDFD EAFAKEITKL NDIVVRGGVE
LEKFKLFDAD PKNEHFVYNS WHSLGAIRKL AGEGRAFYAP IKYSELPKYY RTSIKKPNVF
VTQATPMDEH GNFNFGISAS HLYAAIENSD IVIIEVNKNV PRGLGGFENF VNIKDVDYII
EGSNPEMIAL GKANPSDLDK EVAKYVVEEL VDGACLQIGI GGLPTAIGKE IANSDLKDLG
VHTEMYVDSF VELTKAGKIN GSKKNIDKGR QVYAFAAGSK ELYDFIDNNE QLCAAPVDYC
NGIEQISALD NFMSINSALE VDLNGIVSAE SSGTKHISGS GGALDFMIGA YNSKGGKSFV
TLHSSRVDKK GVRHSNIVPR LIEGTQPTGC RANTHYVATE FGMVNLKGQS LWERTEKLIS
IAHPDFRDDL IKEAESMRIW RKSNK
//
