ID A0A1F7IL41_9BACT Unreviewed; 383 AA.
AC A0A1F7IL41;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2957_01250 {ECO:0000313|EMBL:OGK44071.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_38_11.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802060 {ECO:0000313|EMBL:OGK44071.1, ECO:0000313|Proteomes:UP000179072};
RN [1] {ECO:0000313|EMBL:OGK44071.1, ECO:0000313|Proteomes:UP000179072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGK44071.1}.
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DR EMBL; MGAK01000025; OGK44071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7IL41; -.
DR STRING; 1802060.A2957_01250; -.
DR Proteomes; UP000179072; 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:SF6; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..218
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 257..364
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 383 AA; 41222 MW; 586AADC8DDB7AF83 CRC64;
MINVIGYHTT KFGEQWNKSL FDLISEAIHG VIKEMKIDKE EINAVFFGNM LAGILENNVH
GGSKISEILK THVPMYRVEA ACASGGLAFN LACQYLNANK NSTVLVVGGE KMTDYPTPKV
ITALSAAASG EEQEAGLTFP GLYAMLARIY LHTYGYTEEH LAAVSVKNHF HGTFNDKAQF
QKEISIEDVL KSPYIADPLK VLDASPISDG ASAILVTNNR HIAHRIDKKM TVLSSQAATD
SISLSGRAYL DRLDSTVQAG NKAFSDAKLS PIDISVAEVH DCFSIAEILA MEDLGFFKKG
EGGERMKNYE TMFGKTNGLV VNTSGGLKAS GHPVGATGVK QIGEVFLQLT QQAGKRQVKK
IKYGLTHNVG GSGGTAVVNI FSS
//
