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Database: UniProt
Entry: A0A0N7LRX5_9RHOB
LinkDB: A0A0N7LRX5_9RHOB
Original site: A0A0N7LRX5_9RHOB 
ID   A0A0N7LRX5_9RHOB        Unreviewed;       523 AA.
AC   A0A0N7LRX5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE            EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN   Name=ydiF {ECO:0000313|EMBL:CUH52036.1};
GN   ORFNames=SHM7688_01476 {ECO:0000313|EMBL:CUH52036.1};
OS   Shimia marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH52036.1, ECO:0000313|Proteomes:UP000054823};
RN   [1] {ECO:0000313|EMBL:CUH52036.1, ECO:0000313|Proteomes:UP000054823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH52036.1,
RC   ECO:0000313|Proteomes:UP000054823};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: CoA transferase having broad substrate specificity for short-
CC       chain acyl-CoA thioesters with the activity decreasing when the length
CC       of the carboxylic acid chain exceeds four carbons.
CC       {ECO:0000256|PIRNR:PIRNR000858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + an acyl-CoA = a carboxylate + acetyl-CoA;
CC         Xref=Rhea:RHEA:13381, ChEBI:CHEBI:29067, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58342; EC=2.8.3.8;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000858};
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC       {ECO:0000256|ARBA:ARBA00007154, ECO:0000256|PIRNR:PIRNR000858}.
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DR   EMBL; CYPW01000011; CUH52036.1; -; Genomic_DNA.
DR   RefSeq; WP_058239268.1; NZ_FOMU01000012.1.
DR   AlphaFoldDB; A0A0N7LRX5; -.
DR   STRING; 321267.SHM7688_01476; -.
DR   OrthoDB; 9805230at2; -.
DR   Proteomes; UP000054823; Unassembled WGS sequence.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR   InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR43293; ACETATE COA-TRANSFERASE YDIF; 1.
DR   PANTHER; PTHR43293:SF1; ACETATE COA-TRANSFERASE YDIF; 1.
DR   Pfam; PF01144; CoA_trans; 1.
DR   PIRSF; PIRSF000858; SCOT-t; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054823};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT   ACT_SITE        328
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   523 AA;  56054 MW;  F9539D97CB3E2EBA CRC64;
     MSKVVSPSQA VSQIRDGAVV SVSSSSSLGC PDLVLKAIGA RFEAEGHPQN ITSLHPIAAG
     DMYGVKGMDY LAQDGLLRRV IAGSYPSGPS SLEMPDIWKM IVEDRVAAYN VPSGIMYDMH
     REAAARRPGV LTKVGLQTFV DPIREGCAMN EKAAAAPIVS RTEFGGETWL HFPNIAPDVC
     ILRATTADEH GNLTYEHEGA YLGGLEQAIA ARNNGGLVIA QVSRVTMRGS LRPHDVRVPG
     HLVDLVVLDP DQKQTCETPY DPAISGQVMR PWDSFTLAEY GVEKVIARRA AMELSQGQTA
     NLGFGISAMV PRVLLEEGHP EAVTWAIEQG AVGGVPLTGF AFGCASNADA FVPSPQQFIY
     FQGGGFDMSF LSFLEVDVEG NVNVSKLGKK PYLTAGCGGF VDITARAKKI VFSGWFEAGA
     QMELSEEALR VAKPGKFTKM VDQVEHVTFS GARARETGQE VLYITERCVI RLTDQGLVAT
     EIMPGIDAQA DIVGVTEGRV TVAENAQLMD KRLLAQAPMG LVL
//
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