ID A9WRA1_RENSM Unreviewed; 430 AA.
AC A9WRA1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABY24110.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ABY24110.1};
GN OrderedLocusNames=RSal33209_2384 {ECO:0000313|EMBL:ABY24110.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24110.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP000910; ABY24110.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WRA1; -.
DR STRING; 288705.RSal33209_2384; -.
DR KEGG; rsa:RSal33209_2384; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABY24110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABY24110.1}.
FT DOMAIN 27..289
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 299..419
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 115
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 430 AA; 45883 MW; 7AE3EDC7E0485F65 CRC64;
MEPRRSPESF RKEEQQVSPN TRQVREVVFV DGVRTPFGKT GEKGIYSDVR TDDLVVKCIR
ELMRRNPSLP PERIDEVTIA ATTQTGDQGL TIGRTAALLS GLPKSVPGFA IDRMCAGAMT
AVTTTASGIG FGAYDVVIAG GVEHMGHHPM GSGADPNPRF MSESLVDPAA LNMGNTAENL
HDRFPAITKE RTDRYAVNSQ NKLAAAYEKG QIQPDLVPVA ASKVQPHSAE EKNPGHVWNL
NTVDEPPHPG TTMEDLASLR TPFRPHGRVT AGNAAGLNDG ATAAILASAE AAEELGLTVK
ITMVSYGFAG VEPEVMGIEP VPATEKALKN AGLSIDDIGL FEINEAFAVQ VLSFLDYFGI
ADEDPRVNRY GGAIAVGHPL ASSGVRLMNQ LARQFEEDHS VQYGITTMCI GLGMGAKVIW
ANPHFEGAAA
//
