ID A0A1H4CL48_9SPHI Unreviewed; 392 AA.
AC A0A1H4CL48;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=SAMN05443550_10491 {ECO:0000313|EMBL:SEA61059.1};
OS Pedobacter hartonius.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=425514 {ECO:0000313|EMBL:SEA61059.1, ECO:0000313|Proteomes:UP000198850};
RN [1] {ECO:0000313|EMBL:SEA61059.1, ECO:0000313|Proteomes:UP000198850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19033 {ECO:0000313|EMBL:SEA61059.1,
RC ECO:0000313|Proteomes:UP000198850};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNRA01000004; SEA61059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4CL48; -.
DR STRING; 425514.SAMN05443550_10491; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000198850; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000198850};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SEA61059.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 87
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 40707 MW; 461A434DE7B9B983 CRC64;
MREVVIVSAL RTPIGSFGGV LSGFTATQLG GFAIKAAVAQ AGVQPGDIQE VFMGNVLSAS
LGQAPATQAA KYAGLPDMPA TTINKVCASG TKAIMLAAQS IALGQNDIVV AGGMESMSNV
PYYLDKARTG YRLGHGQMTD GLVKDGLWDV YNDYHMGAAA ELCASTCGIS REDQDNYAAG
SYRRAQLAQE TGKFTDEIIP LEVTDRKGNT TVVNKDEDPY TVNFDKIPGL KPVFKKDGTV
TAANASALND GAAALVLMSA EKAAELGLKP MARILSYADA QQAPEWFTTA PSKAIPLALQ
RAGKNIDDVD FFEINEAFSV VSLANNKELG LTEDVVNVNG GAVAMGHPLG ASGARIIVTL
LSVLNQNNGK IGVAGICNGG GGASAMVIEN LN
//
