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Database: UniProt
Entry: A0A0R2U7L4_9GAMM
LinkDB: A0A0R2U7L4_9GAMM
Original site: A0A0R2U7L4_9GAMM 
ID   A0A0R2U7L4_9GAMM        Unreviewed;       411 AA.
AC   A0A0R2U7L4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRO95220.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:KRO95220.1};
GN   ORFNames=ABS10_07490 {ECO:0000313|EMBL:KRO95220.1};
OS   SAR86 cluster bacterium BACL1 MAG-120820-bin45.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1655612 {ECO:0000313|EMBL:KRO95220.1, ECO:0000313|Proteomes:UP000051027};
RN   [1] {ECO:0000313|EMBL:KRO95220.1, ECO:0000313|Proteomes:UP000051027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL1 MAG-120820-bin45 {ECO:0000313|EMBL:KRO95220.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO95220.1}.
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DR   EMBL; LICS01000042; KRO95220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2U7L4; -.
DR   STRING; 1655612.ABS10_07490; -.
DR   Proteomes; UP000051027; Unassembled WGS sequence.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KRO95220.1};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRO95220.1}.
FT   DOMAIN          6..190
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          286..385
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   411 AA;  45297 MW;  1E54BE6304928730 CRC64;
     MQKRVYILGG YQSDFAQNWY RNELDLLDVF EETIAKGLQS VDLEPKDVDV AHVGNFTAEL
     FCNQGHLGGF FVSSHPDFFG LPSSRHEAAC ASGSIATLAA CAEIESGRYE LAAVLGIEQM
     RNVSGEQAAQ NIGGPAMRSG FECQGVKYPW PHMFSELTNE YDKRYGINED HLSRISEINF
     FNAKKNPNSQ TRGWTFESDT FTRSDHTNPV IEGRTRKMDC GQVTDGAAII FLASERKARE
     YAKIRSMNFE SIPYIKGWGH QTGPITYQEK IDFSQDKEYV FPHVKKAIDD AFKRASMQGV
     TDIDGIETHD CFTSTEYMAI DHFGITKPGE SWKAIESGDI EIGGKIPINA SGGLIGLGHP
     VGATGVRMLL DSYKQCTNNA GDYQINNAKN ISTLNIGGSA TTVVSFVVGT I
//
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