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Database: UniProt
Entry: F7XEH9_SINMM
LinkDB: F7XEH9_SINMM
Original site: F7XEH9_SINMM 
ID   F7XEH9_SINMM            Unreviewed;       523 AA.
AC   F7XEH9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE            EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN   OrderedLocusNames=SM11_pC0881 {ECO:0000313|EMBL:AEH81954.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH81954.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH81954.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH81954.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH81954.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
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; CP001831; AEH81954.1; -; Genomic_DNA.
DR   RefSeq; WP_010967743.1; NZ_JAJJBH010000005.1.
DR   AlphaFoldDB; F7XEH9; -.
DR   GeneID; 61599540; -.
DR   KEGG; smx:SM11_pC0881; -.
DR   PATRIC; fig|707241.3.peg.4845; -.
DR   HOGENOM; CLU_026774_4_0_5; -.
DR   OMA; QRRYIAS; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11c.
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   Plasmid {ECO:0000313|EMBL:AEH81954.1};
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;  55902 MW;  794502C421AE7F87 CRC64;
     MAKVMTANEA AGLVRDGAVL AVNSSSGLGC PDEVLKALGE RFELEGHPRG LTSVHPIAAG
     DFFGTKGVDH IARRGMLKKI IGGSYPSGPS NAEPPLIWQM ILKEEVAAWN VPSGIVFDML
     REGAAKRPGV LTKVGIDTFV DPEQEGCAMN AAARSEPIVR RVRFADDDWL HFPPIQPDVA
     IIRATTADER GNLTFEHEGA TLGAMEMALA ARNSGGIVIA QVKRVAAEGT MRPHDVRVPG
     ILVDVIVEAP DQLQTTATPY DPAISGELFR PLHTFRTPAL DPGKVIARRV AQELKAGWAV
     NIGFGISANV PRVLIEEGHH GKITWVIEQG AVGGVPLLDF KFGCASNAEA FVASPHQFCY
     FQAGGFDCSL LSFLEIDAEG SVNVSRLAAT PHRTAGAGGF VDITARARKI VFSGNFNAGA
     KMRIEDGRLV IDKEGRIAKI VPKVDQVSFS GRRARVQGQD VTYVTERCVM KLEPDGLVVS
     EVAPGLDLRR DVLDQAATPL RVADGLKEMD QALFLSTAMG LGL
//
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