ID A0A1S9MHH7_9MICC Unreviewed; 430 AA.
AC A0A1S9MHH7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OOP64721.1};
GN ORFNames=BMF89_02455 {ECO:0000313|EMBL:OOP64721.1};
OS Arthrobacter sp. SRS-W-1-2016.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1930254 {ECO:0000313|EMBL:OOP64721.1, ECO:0000313|Proteomes:UP000190514};
RN [1] {ECO:0000313|EMBL:OOP64721.1, ECO:0000313|Proteomes:UP000190514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-1-2016 {ECO:0000313|EMBL:OOP64721.1,
RC ECO:0000313|Proteomes:UP000190514};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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:OOP64721.1}.
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DR EMBL; MTPV01000010; OOP64721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9MHH7; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000190514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000190514};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OOP64721.1}.
FT DOMAIN 16..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..400
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 430 AA; 45000 MW; 5816D329F721242C CRC64;
MSQTGNSATP RTVRDVVFVD GVRTPFGKAG DKGIYAGTRA DDLVVKCIRE LMRRNPSLPA
ERVDEVAIAA TTQTGDQGLT IGRTAALLAG LPRSVPGFAI DRMCAGAMTA VTTTASGIGF
GAYDVVIAGG VEHMGNHPMG AGADPNPRLM SERIVDPAAL NMGNTAENLH DRFPSITKER
TDTYAAASQA KLATAYGKGR IQPDLVPVAT MKPGQGWTVN TVDEPPRPGT TVDDLSELRT
PFRAHGRVTA GNAAGLNDGA TAAVLASAEA AEELGLSVKM RLVSYAFAGV EPEVMGIGPV
PATEKALKNA GLGIEDIGLF EINEAFAVQV LSFLDHFGIA DDDPRVNRYG GAIAVGHPLA
SSGVRLMNQL ARQFEEDPSV RYGITTMCIG LGMGATVIWE NPHHPSYNGH TIDHSETRTA
ADTESKGAAA
//
