ID A0A3S0XH93_CHLFR Unreviewed; 397 AA.
AC A0A3S0XH93;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:RUR72867.1};
GN ORFNames=PCC6912_60090 {ECO:0000313|EMBL:RUR72867.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR72867.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR72867.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR72867.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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:RUR72867.1}.
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DR EMBL; RSCJ01000041; RUR72867.1; -; Genomic_DNA.
DR RefSeq; WP_016874907.1; NZ_RSCJ01000041.1.
DR AlphaFoldDB; A0A3S0XH93; -.
DR STRING; 211165.GCA_000317285_04534; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000268857; 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; -; 2.
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; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RUR72867.1}.
FT DOMAIN 5..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 274..395
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 397 AA; 41827 MW; 2BD199F001B72FCA CRC64;
MEQAYIISAV RTPLGRFGGT LANFSPIDLG AKAMRAALET AGVSGELVDL YVFGNVLRSG
HGQLLPRQAA FKAGIPETAN GYAVDMVCSS GMIGVMNATL AIRSGEADIV LAGGMESMSQ
AGFSLSHRAR WGYKFLLGAP EQLTDILLRD GLSDGTTGEG MGEQTERIAQ IHGFARKDLD
EIALNSHQRA AAATEKGIFK KEIVPIEVST KKGTQIIDTD EGIRADTSLE ALAKLRPAFN
KDGVLTAGNS SQISDGAAAL ILASQSAVDK YGLKPIAKVI GSSWQGGETW RFVEIPVLAV
KKLLDKLNLK ISDFDLFENN EAFAVNSLLF HHLLGIPLER LNVNGGAIAL GHPIGASGAR
ILVTLLNALE QEDGQLGLAA ICHGTGGGTA IAIERLK
//
