ID A0A0Q6WHK4_9BURK Unreviewed; 522 AA.
AC A0A0Q6WHK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN ORFNames=ASC87_07835 {ECO:0000313|EMBL:KQV85584.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV85584.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV85584.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV85584.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV85584.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV85584.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQV85584.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMDI01000045; KQV85584.1; -; Genomic_DNA.
DR RefSeq; WP_056669354.1; NZ_LMDI01000045.1.
DR AlphaFoldDB; A0A0Q6WHK4; -.
DR STRING; 1736433.ASC87_07835; -.
DR OrthoDB; 9805230at2; -.
DR Proteomes; UP000051465; 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; 2.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051465};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 322
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 522 AA; 54986 MW; 4B5137F761AC2862 CRC64;
MKIITADQVG PLVKDGATLF LGGLAMMGLA EEVLQGLERH FLATGHPSQL TTWACGAIGN
AGSGGMAHLA HPGMVKRVVA GHFGQTGKAM MAMVHAGEIE AYNFPQGSLC SLTRHIASRS
PGLLTKVGLG TFVDPRLEGG KLNTASREDL VRLVEFDGEE WLFHPTPHID VAFIRATYAD
ERGNLSMDKE GILLDQLAVA QAARACGGIV VAQVEAVVAA GSLHPKSVKV PGLVVDYVVV
AKPENHLQTI TTAFNPAFSG DVRVPLGSVP ALPLDERKVI ARRAAMELQP GAVTNLGIGI
PAGIPGVAAE EGVAGLLSLS VECGVNGGVP AQGGDFGLAY NAESIIEQSS QFDFYDGGGL
DCSFLGLAQT DRHGNVNVSK FNGRPVGCGG FINITATTPR LVFCGSFTAG GVDLAVADGQ
LNIRQEGRSR KFVEQVEQIT FNGRDAARRG QEVLFVTERA VFALRPDGLE LTEIAPGIDL
ERDVLAQMEF RPLMRDVKTM DAGLFREHWG GLAAALSTPT HA
//
