ID M7A084_9ACTN Unreviewed; 378 AA.
AC M7A084;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EMP11726.2};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EMP11726.2};
GN ORFNames=ISGA_1450 {ECO:0000313|EMBL:EMP11726.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP11726.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP11726.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP11726.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(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:EMP11726.2}.
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DR EMBL; APHK02000090; EMP11726.2; -; Genomic_DNA.
DR RefSeq; WP_053778269.1; NZ_CP132196.1.
DR AlphaFoldDB; M7A084; -.
DR STRING; 1241906.ISGA_1450; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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:EMP11726.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EMP11726.2}.
FT DOMAIN 5..246
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 255..375
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 378 AA; 38473 MW; 7FCE76FA082E9DD3 CRC64;
MTDAVIVDAV RTPIGRRGGA LSGIHPADLS AHVLEALAAR TGVDPAVVDD VMWGCVSQSG
EQAGNIARTA VLAAGWPQSV PGTTVTRACG SSQQTLAMAA AAVISGQLDI VVAGGVESMS
RVPMGSAAPN GESQPATVLD RFGVDRFSQG IGAEMVARRW DLDRTRVDEY SLRSHELAAA
AADSGAFDAQ LATLPGVLEG DEGIRRGGTL ESLGKLKTVF DENGVIHAGN ASQISDGAGA
LLVMSSETAA AHGLTPIARV HTTVVAADDP VIMLTGPIPA TAKALARSGL TIDEIGAFEV
NEAFAPVPLA WQIETGAADK ALNPLGGAIA VGHPLGGSGA ILATRLIHHM RDNGIRYGLQ
TMCEAGGMAN ATIFELVG
//
