ID L8LMI8_9CHRO Unreviewed; 396 AA.
AC L8LMI8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ELR98072.1};
GN ORFNames=GLO73106DRAFT_00018940 {ECO:0000313|EMBL:ELR98072.1};
OS Gloeocapsa sp. PCC 73106.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR98072.1, ECO:0000313|Proteomes:UP000011180};
RN [1] {ECO:0000313|EMBL:ELR98072.1, ECO:0000313|Proteomes:UP000011180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR98072.1,
RC ECO:0000313|Proteomes:UP000011180};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELR98072.1}.
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DR EMBL; ALVY01000193; ELR98072.1; -; Genomic_DNA.
DR RefSeq; WP_006529089.1; NZ_ALVY01000193.1.
DR AlphaFoldDB; L8LMI8; -.
DR STRING; 102232.GLO73106DRAFT_00018940; -.
DR PATRIC; fig|102232.3.peg.2112; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000011180; 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:UP000011180};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ELR98072.1}.
FT DOMAIN 4..265
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 396 AA; 42317 MW; 3BDCE8E41C09EBC3 CRC64;
MRDVYLVSAV RTPLGRFGGN LLNFSAVDLG AHVMKAAIAQ AGIPPQLIDI YIMGNVLRAG
HGQLLPRQAA LKAGIPDTVN GYGIDMVCSS GMMSLINGIN HIKVGDADLV LAGGMESMSQ
TGFALSYRAR WGYKLLLQQP EELTDLLVCD GLTDGTTKET MGEQAERLAQ EHGFTRTELD
EIALSSHQRA VAAIERGSHR NEIAPIAINS KKGTQTVEQD EGIRPDTNLE ILGKLSPVFS
PEGVLTAGNC SQISDGAAAV ILASQEAIAR YGLQPIAKVL GSAWEGGETW RFPEYPVYAA
KKLLYKLEMN LSDFDMFENN EAFALSNLLF TRILGVSPDK LNVNGGSIAL GHPIGSSGTR
IVVTLLHALK EYNQTRGLAA ICHGTGGGTA LAFERV
//
