ID A0A257B6I4_9BACT Unreviewed; 393 AA.
AC A0A257B6I4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OYT72517.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:OYT72517.1};
GN ORFNames=CFK52_04770 {ECO:0000313|EMBL:OYT72517.1};
OS Chloracidobacterium sp. CP2_5A.
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT72517.1, ECO:0000313|Proteomes:UP000216393};
RN [1] {ECO:0000313|EMBL:OYT72517.1, ECO:0000313|Proteomes:UP000216393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP2_5A {ECO:0000313|EMBL:OYT72517.1};
RA Ward L.M., Mcglynn S.E., Fischer W.;
RT "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT Acidobacteria from a Japanese hot spring.";
RL Submitted (JUN-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:OYT72517.1}.
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DR EMBL; NKPT01000009; OYT72517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257B6I4; -.
DR Proteomes; UP000216393; 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; IPR020615; Thiolase_acyl_enz_int_AS.
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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:OYT72517.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OYT72517.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
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 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; 40609 MW; 7C018528C1BA377E CRC64;
MPASVILSAV RLPIGKFQGS LKSFAAPALG SKVVRAAIER AGIDAIQVDE VVMGCVLQAG
LGQNPARQAA LGAGLPPAAA ALTVNQVCGS GLRAVMLAAQ AIQAGDAEFV VAGGMESMTN
APYVLPKARE GYRMGHGEIV DVMIHDGLWC AFENWHMGCT AEVVAERYRV SREAQDAFAA
DSQAKAIAAQ QAGAFRAEIE PVTIPQRKGD PVVFTEDEGP RADTTVATLA KLRPAFQPDG
TVTAGNASTI NDGAAAVVVA SEAQAERLGR QPLARIVAQA MSGIEPKLIM MAPVEATRRV
LAKAGWRADD VDLFEFNEAF AAQAIAVTRE VGADPAKVNV NGGAIALGHP IGASGARVLV
TLLHAMQARQ VKRGVAALCL GGGNAVALAV ERD
//
