ID J9SRI7_9ACTN Unreviewed; 408 AA.
AC J9SRI7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AFR50963.1};
GN ORFNames=KTR9_4356 {ECO:0000313|EMBL:AFR50963.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR50963.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR50963.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR50963.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002907; AFR50963.1; -; Genomic_DNA.
DR RefSeq; WP_014928383.1; NC_018581.1.
DR AlphaFoldDB; J9SRI7; -.
DR STRING; 337191.KTR9_4356; -.
DR KEGG; gor:KTR9_4356; -.
DR PATRIC; fig|337191.3.peg.4761; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_11; -.
DR Proteomes; UP000003281; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; -; 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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AFR50963.1}.
FT DOMAIN 5..274
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 282..405
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 408 AA; 42639 MW; 999215590F2A1269 CRC64;
MTEAVIVAAA RSPIGRARKG SLKDMRPDDL AAQMVRAALD QVPALDPRQI DDLMLGCGLP
GGEQGYNMGR VVSVLLGLDS VPGTTITRYC SSSVQTTRMA LHAIKAGEGD VFISAGVETV
SRYDKGSADE LPGTHNPVFA DAEARTVATA DSGTDAWTDP RDDGALPDVY IAMGQTAENL
ARAKNVTRED MDLFGVRSHN LVEQAIADGF YAQEITPVTL PDGTVVRTDD GPRSGVTYDA
VAQLKPVFRP DGLVTAGNCC PLNDGAAALV VMSDTKARDL GLTPLARVIS TGVTGLSPEI
MGYGPVEASK QALARAGMTI DDVDLVELNE AFAAQVIPSA RDLGIDPFGD KLNVHGGAIA
VGHPFGMTGA RITTTLLNGL RAKDKSIGLE TMCVGGGQGM AIIYERLS
//
