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
//