ID F4CEC8_SPHS2 Unreviewed; 393 AA.
AC F4CEC8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN OrderedLocusNames=Sph21_2475 {ECO:0000313|EMBL:ADZ79029.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79029.1};
RN [1] {ECO:0000313|EMBL:ADZ79029.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ79029.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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}.
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; CP002584; ADZ79029.1; -; Genomic_DNA.
DR AlphaFoldDB; F4CEC8; -.
DR STRING; 743722.Sph21_2475; -.
DR KEGG; shg:Sph21_2475; -.
DR PATRIC; fig|743722.3.peg.2650; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_1_10; -.
DR OrthoDB; 9764892at2; -.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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.
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:ADZ79029.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ADZ79029.1}.
FT DOMAIN 5..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..391
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 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 41435 MW; D2DAA0B02F6FBBBB CRC64;
MTNEVYIVSA ARTPIGSFGG SLAGFTATQL GGLAVKEAVK RASLLADDIQ EAYIGNVLSA
NLGQAPATQV IKLAGLGNIP ATTVNKVCAS GTKAVMLAAQ NIALGHQDII IAGGTESMSN
VPYYLDKART GYRLGHQQAI DGLIRDGLWD VYNDYHMGSA AELCASSCKI SREEQDQYAI
SSYKRAQKAE RNGKFKQEII PLEVTDKKGN STTIDTDEEI NNVFFDKISS LKPVFQKEGT
VTAANASTLN DGAAALVLMS KAKAEQLGVK PLARILGYAD AQQDPEWFTT APAQAIPLAL
ERAGVSAKEV DYYEINEAFS VVSIANNQLL QLDPEKVNIY GGAVSLGHPL GASGARILVT
LLSVLRQEDG DLGVVGICNG GGGASALVIE RLS
//
