ID A0A0N1AA55_9PROT Unreviewed; 555 AA.
AC A0A0N1AA55;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN ORFNames=IP80_14595 {ECO:0000313|EMBL:KPF47134.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF47134.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF47134.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF47134.1,
RC ECO:0000313|Proteomes:UP000037849};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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:KPF47134.1}.
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DR EMBL; LJHW01000027; KPF47134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1AA55; -.
DR STRING; 1523424.IP80_14595; -.
DR PATRIC; fig|1523424.3.peg.1927; -.
DR OrthoDB; 9805230at2; -.
DR Proteomes; UP000037849; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037849};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 351
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 555 AA; 57703 MW; DEFF79A70F09ECBE CRC64;
MKAPGPRWLS ADEAAALVQP GWTVASAGFV GAGHAEAVTE ALERRYLATG APRDLTLVYS
AGQGDRSQRG VNHFGNPGMV KAVCGGHWRS ATRLSALALA EGCAAWNLPQ GVITHLYRAI
AAGQPGLLSR VGLHTFVDPR TALDARYQGG ALNQRALAAM ALPAAAGGRH WVEALTLRGE
DFLFYPSFPI HCAVLRATAA DARGNLSAHG EAFHHELLAL AQATRNSGGL VIAQVRERVP
HHAALAPIRV PGHLVDVVVH NTDPELHSIT FGEQENEAYL HPWRGDTAAA APAALEGPLD
ARTLVQRRAV LELAAGGTGA HRVVNLGVGM PAAVGAMAQA AGVGGYTLSV EAGPIGGTPA
DGLSFGASAW PEAVVDQPAQ FDFYDGGGID LAVLGMAELD AAGNVNVSRF GSGEQALIAG
VGGFINITQG AKALVFVGTL TAGGLQVQAE GGRLRIVQEG RLKKLVPAVA HLSYNAAYMA
ARGQLVRYIT ERAVFEMRPD PQAAPGSAPR LTLIEIAPGL DLQRDVLDVC GAPVAVAADL
REMDARIFSS APFRL
//
