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Database: UniProt
Entry: A0A0S8KAP4_9CHLR
LinkDB: A0A0S8KAP4_9CHLR
Original site: A0A0S8KAP4_9CHLR 
ID   A0A0S8KAP4_9CHLR        Unreviewed;       393 AA.
AC   A0A0S8KAP4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KPL18419.1};
GN   ORFNames=AMJ93_13845 {ECO:0000313|EMBL:KPL18419.1};
OS   Anaerolineae bacterium SM23_84.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL18419.1, ECO:0000313|Proteomes:UP000052016};
RN   [1] {ECO:0000313|EMBL:KPL18419.1, ECO:0000313|Proteomes:UP000052016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_84 {ECO:0000313|EMBL:KPL18419.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {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:KPL18419.1}.
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DR   EMBL; LJUZ01000253; KPL18419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8KAP4; -.
DR   PATRIC; fig|1703388.3.peg.2710; -.
DR   Proteomes; UP000052016; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00829; SCP-x_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; IPR020616; Thiolase_N.
DR   PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 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; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPL18419.1}.
FT   DOMAIN          4..230
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          268..367
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   393 AA;  41595 MW;  C85E58DB027024B0 CRC64;
     MRKVAIIGVG MIPFGRRDED SLVDMLAYAA LNAMDDAGLG ERPIDAVYVG NMGAGLFNHQ
     SAVASALVDR LNLLPAAADT VENGPASGGS AIKNGVLAVA SGHFDLVLVA GGEKMREVIG
     PRATDIVATM THPQAEYIYG ATLPTMAGLF TRLYMKEYGV TSEHLARVAI KNHRNGLLNP
     YAHIHALITM EGILTSPHAI VNNPIVADPI RLYDCCPVSD GAAACLLCPA EMAREFGKPA
     IVVAGFGQAT DTHTLQERED PTDLKAVRIA AQQAFETAQL KPKDIDVAEL HDAFTILEIA
     ESEHAGFFKK GEGAKALDEG QTEIGGKLPI NPSGGLKARG HPLGATGVAQ VVELVWQLRG
     EAGERQVKGA EKGFSLNFGG FGNNVVSFVL RRE
//
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