ID A0A0R2UAI4_9GAMM Unreviewed; 393 AA.
AC A0A0R2UAI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRO96486.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRO96486.1};
GN ORFNames=ABS10_03830 {ECO:0000313|EMBL:KRO96486.1};
OS SAR86 cluster bacterium BACL1 MAG-120820-bin45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1655612 {ECO:0000313|EMBL:KRO96486.1, ECO:0000313|Proteomes:UP000051027};
RN [1] {ECO:0000313|EMBL:KRO96486.1, ECO:0000313|Proteomes:UP000051027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120820-bin45 {ECO:0000313|EMBL:KRO96486.1};
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|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:KRO96486.1}.
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DR EMBL; LICS01000001; KRO96486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2UAI4; -.
DR STRING; 1655612.ABS10_03830; -.
DR Proteomes; UP000051027; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase 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; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRO96486.1}.
FT DOMAIN 7..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..392
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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 41234 MW; A7C8353A99128917 CRC64;
MSNNNAYIVS AVRTAGGKKN GSLSQWHPAD LGAKVLDELV LQTGIDPALI DDVIFGCVDQ
VGAQSGNVAR NAVLASSLPE SVPGTSVDRQ CGSSQQAIHF AIQAVMSGTQ DVVIGGGVEI
MSMVPIGASI KDGYEAGHGL PFDSVGMKAR YPGVYFSQFT GAEMMAKKWN LSREDLDNFA
FSSHQKAIAA VHGKYFDREI LPVQAKNAEG KTDMIFLDEG IRYDASLEAL AGLKTVTEGG
VITAGNASQI TDGAAAVMVC NDAGLKKIKT DPRARIVAIS VVGDDPIMML GAPIPASHKV
LKAAGLNIND IDLYEINEAF APVPLSWAID LKADKDKLNV NGGAMALGHP LGATGAKLMT
TLLHELERRD GKYGLQAICE GGGTANATII ERL
//
