ID I2GTC0_9BACT Unreviewed; 402 AA.
AC I2GTC0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:CCH57149.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:CCH57149.1};
GN ORFNames=BN8_06553 {ECO:0000313|EMBL:CCH57149.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH57149.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH57149.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(2012).
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:CCH57149.1}.
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; CAIT01000010; CCH57149.1; -; Genomic_DNA.
DR RefSeq; WP_009285710.1; NZ_CAIT01000010.1.
DR AlphaFoldDB; I2GTC0; -.
DR STRING; 1185876.BN8_06553; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000009309; Unassembled WGS sequence.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:CCH57149.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009309};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CCH57149.1}.
FT DOMAIN 6..229
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..400
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 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 402 AA; 42625 MW; 54DBFDD5F2FF2FCE CRC64;
MAEAFVYDAV RTPRGRGKSD GSLHDVQPIQ LLTSVLRELR DRNELDTTLI DDVIMGCVTP
IGEQGADIAR TAALEAGYAE SVAGVQLNRF CSSGLEAINM AAAYVMSGQV DAVVAGGVES
MSRVPMGSDG GALFMNPQIV ARHNIVPQGI SADLIATKYG YSRQDVDTFA AESYRRATVS
QQEGRFHKTL VPVRDEIGVT LLDRDEGVRP DTTAESLSKL KPAFEAMGQM GLDALALLKY
AQYDRINHVH HAGNSSQIVD GAAGVLIGSR TFGEQAGLKP RARIKAFAIV GSEPTIMLTG
PLPATKKVLK RAGMQISDID LFEVNEAFAA VPLLFMDEFG VDHSKLNVNG GAIALGHPLG
ATGAIISATL IDELERSGKQ VGLSTLCIGG GMGIATIFER VN
//
