ID A0A257SV88_9GAMM Unreviewed; 438 AA.
AC A0A257SV88;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OYV76186.1};
GN ORFNames=B7Z66_09530 {ECO:0000313|EMBL:OYV76186.1};
OS Chromatiales bacterium 21-64-14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales.
OX NCBI_TaxID=1970504 {ECO:0000313|EMBL:OYV76186.1, ECO:0000313|Proteomes:UP000215939};
RN [1] {ECO:0000313|EMBL:OYV76186.1, ECO:0000313|Proteomes:UP000215939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-64-14 {ECO:0000313|EMBL:OYV76186.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYV76186.1}.
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DR EMBL; NCBI01000018; OYV76186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257SV88; -.
DR Proteomes; UP000215939; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OYV76186.1}.
FT DOMAIN 14..288
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 297..435
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 438 AA; 46991 MW; F15D0DEBEA76F8AF CRC64;
MTQRKHSGYP GRAVYVVDGS RTPQLKAKDR PGAFAAADLA VAAGRPLLAR QPFEPPDLDE
VILGCVMPNA DEANIGRIAA LRLGCGKRVP GWTVQRNCAS GMQALDCAAR NIADGRSDLV
LAGGVEAMSH APVLLGEAMV AWLGAWRGAR SFGQRIKALS QLRPRHFQLI IGLLRGLTDP
VVGLSMGQTA ENVAYRFGIS RDTMDQLALE SHRRLAEAQD QGRLANEVEV IFDSRGHHYD
FDDGLRRDTD LAKLARLRPV FDRPFGLVTA GNSAQITDGA AWLILACEEV IQRHQLPVLG
RIVDCSWAAL DPAQMGLGPV HASTPLLESH GLALQDVDYW ELNEAFAAQV LACLAAWEDE
DYCRAELGQK NALGSIDRSR LNVDGGGIAL GHPIGATGAR IVLHLLHVLE REGARRGIAT
LCIGGGQGGA MLVERDGG
//
