ID R7WNT4_9NOCA Unreviewed; 407 AA.
AC R7WNT4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EOM76973.1};
GN ORFNames=Rrhod_1592 {ECO:0000313|EMBL:EOM76973.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM76973.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM76973.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM76973.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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:EOM76973.1}.
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DR EMBL; APMY01000054; EOM76973.1; -; Genomic_DNA.
DR RefSeq; WP_010837656.1; NZ_APMY01000054.1.
DR AlphaFoldDB; R7WNT4; -.
DR PATRIC; fig|1273125.3.peg.1537; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 4440515at2; -.
DR Proteomes; UP000013525; Unassembled WGS sequence.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EOM76973.1}.
FT DOMAIN 4..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..405
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 42219 MW; 91E2DFE052EBFDEF CRC64;
MRDVVVCEPV RTPIGRYGGA VASLTAAELG TIALRGLLDR TGLAPEAIED VILGHCNATS
EAPAIGRVVA LDAGLPITVP GMHIDRRCGS GLQAVIQAAM QVGTGNDDVV VAGGTESMSN
ASFYSVDMRW GGARSGIAMH DSLARARSTA GGKHHPVAGG MIETAENLRK QYEITREEQD
ELAVASHLRA VRAQKDGVLA EEIVPVAVQT KGGEQIVDTD EHPRPDVSLD SLARLKPIMA
KADPAATVTA GNASGQNDAA AMCIVTTPEV AERHGLRPLV RLVSWGLAGV PPSTMGIGPV
PATAAALGKA GLTLADIDVI ELNEAFAAQA LAVTREWGFG RFGEGGDFDR TNVHGSGISL
GHPVGATGVR MLASLARELD RREARYGRET MCIGGGQGLA AVFERVA
//
