ID W0EDD8_9FIRM Unreviewed; 442 AA.
AC W0EDD8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=DESME_11450 {ECO:0000313|EMBL:AHF07553.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF07553.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF07553.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007032; AHF07553.1; -; Genomic_DNA.
DR RefSeq; WP_006718196.1; NZ_CP007032.1.
DR AlphaFoldDB; W0EDD8; -.
DR STRING; 871968.DESME_11450; -.
DR KEGG; dmt:DESME_11450; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000010847; Chromosome.
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:UP000010847};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03228}.
FT DOMAIN 5..182
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 276..431
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 242
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 217..221
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 317
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 340
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
SQ SEQUENCE 442 AA; 49145 MW; F64137B7ADA5DDA0 CRC64;
MSYSGEYQKK LVTPEEAVRV VKSGDWVDYG AFAGQVVALD KALAARKEEL FDVKIRAVTA
LRAPEVVKAD PEAKHFIYNN WHFSGIDRKL HDKGLCYHIP LLYHELPGYY RRFADVDVAM
LPVTPIDEHG FFNFGPQVSH AKATCEKSKV IILEVNPNIP RCLGGKEESI HISQVDYIVE
SNWTLPQIPS GAPTEIESKI ASYIMPELED GSCIQLGIGG MPNAVGQMIA QSDLNNLGLH
SEMFTESMVD MVESGRVTGA NKTTDRYKIA YTFAFGTQKT YNFLNNNPMC AIYPVDYVND
PFIIAQNEKV ISINNCIEVD LTGQVCSESS GTRQISGTGG QFDFAFGSYR SKGGKSFIAM
ESTFKKGDEL RSRIKPSLTP GAIVTTHRAI VHYLVTEYGI VNLKGKSTWE RAEALISIAH
PNVREDLIKE AENLGIWRRS NK
//
