ID F2JXD7_MARM1 Unreviewed; 518 AA.
AC F2JXD7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Acetate CoA-transferase YdiF {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.8 {ECO:0000256|PIRNR:PIRNR000858};
GN OrderedLocusNames=Marme_2605 {ECO:0000313|EMBL:ADZ91837.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91837.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ91837.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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; CP002583; ADZ91837.1; -; Genomic_DNA.
DR RefSeq; WP_013661740.1; NZ_CP047696.1.
DR AlphaFoldDB; F2JXD7; -.
DR STRING; 717774.Marme_2605; -.
DR KEGG; mme:Marme_2605; -.
DR PATRIC; fig|717774.3.peg.2690; -.
DR eggNOG; COG4670; Bacteria.
DR HOGENOM; CLU_026774_4_0_6; -.
DR OrthoDB; 9805230at2; -.
DR Proteomes; UP000001062; Chromosome.
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:UP000001062};
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 518 AA; 55823 MW; 18B50F61CEF82DA1 CRC64;
MSKIISLEKA AELIPDNASV AWSTIGMSFF AEAVAKSVEQ RFLETGHPQN LTLIHDCGCG
DGKGKGMSHL AYEGLVKRLI SGHTGQAPKM ANMISEDEIE AYLLPQGVLT TMWRQIAGNK
PGVITKIGMG TYVDPLVSGG KVTSLAKEDL VKRISIEEEE WLLYKTFPLD VVVIRATTAD
EDGNLSVEEE AMLAEILPMA QAVKNRGGIV IAQVKFIAER HSIHPKEVKV PGVLVDYITV
APEEDHMQTI GTTYNPGLAG NSRVPLNAIP PMPFSDRKVI ARRAAMELES NVMVNLGIGM
PDGVASVAAE EQVTRHFTLT TELGTYGGIP ASGPDFGAAW NADAIIEHEA QFDFYDGGGL
DIAFLGLAQA DQLGNLNVSK FGPKVVGPGG FINISQSAKK VVFCGTLENG AKLSFENGQA
KVIQEGKVKK FVQSVDHITF SGAVAQANKK PVLFITERCV LELREEGMVL TEIAPGLDLE
RDVLSAMAFT PIIAEDLKTM PEEIFQESWG GLEKYIIG
//
