ID C1B612_RHOOB Unreviewed; 401 AA.
AC C1B612;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN OrderedLocusNames=ROP_71760 {ECO:0000313|EMBL:BAH55423.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55423.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH55423.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH55423.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH55423.1; -; Genomic_DNA.
DR RefSeq; WP_015890838.1; NC_012522.1.
DR AlphaFoldDB; C1B612; -.
DR STRING; 632772.ROP_71760; -.
DR KEGG; rop:ROP_71760; -.
DR PATRIC; fig|632772.20.peg.7488; -.
DR HOGENOM; CLU_031026_2_1_11; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:BAH55423.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:BAH55423.1}.
FT DOMAIN 10..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 274..395
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 401 AA; 41165 MW; E19B924E29FDBE11 CRC64;
MSESGKIEAV IVAGARTPIA TAFKGTLRDT TAMELARVVL EEVQKRSGLE VSQIDDVILA
ESNYGGGDIA RHAAVVAGML QVPGQAVNRH CAGSLTAIGH AAASVIAGAE RAVIAGGTQS
TSTGPLQKFR TPGTVDEFTD KWMPPTHPDS AEAPNMDMSI TVGWNTAREV GITREEMDAW
ALRSHERALA AIDSGAFADE IVPVQALQPD GSVVEFSTDE HPRRGSTAEK LASLKVLHPE
IEDFSITAGN ASGINDAAAA VAIVGSDLVA EAGLTPLATV KSWAATAVDP ARTGLAVLDV
IPKVLDRAGI SIADVALWEI NEAFASVPVA ACKKLGIDES IVNTAGSGCS LGHPVAASGA
RMVVTLMNEL RRRGGGYGVA AMCAGGGQAG AVVIEVPVPK D
//
