ID A0A0Q9MVA8_9MICC Unreviewed; 428 AA.
AC A0A0Q9MVA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRE65737.1};
GN ORFNames=ASG92_17370 {ECO:0000313|EMBL:KRE65737.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE65737.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE65737.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE65737.1,
RC ECO:0000313|Proteomes:UP000051775};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE65737.1}.
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DR EMBL; LMSB01000007; KRE65737.1; -; Genomic_DNA.
DR RefSeq; WP_056625984.1; NZ_LMSB01000007.1.
DR AlphaFoldDB; A0A0Q9MVA8; -.
DR STRING; 1736395.ASG92_17370; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000051775; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRE65737.1}.
FT DOMAIN 16..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 279..400
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 409..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
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 428 AA; 44686 MW; 7ED8E94D05785DA7 CRC64;
MSQHRSSGNQ RMVRDVVFVD GVRTPFGRAG EKGIYAGMRA DDLVVKCIRE LMRRNPALPA
ERIDEVAVAA TTQTGDQGLT IGRTAALLAG LPRTVPGFAI DRMCAGAMTA VTTTASGIGF
GAYDVVIAGG VEHMGNHPMG AGADPNPRFV SERLVDPAAL NMGNTAENLH DRFPRITKDR
TDAYAVASQN KLAAAYGNGL IQPDLVPVAT MKPGQGWTVN TVDEPPRPGT TVEDLAALRT
PFRAHGRVTA GNAAGLNDGA TAALLASSDA AAELGLPVRM RLVSYAYAGV EPEVMGIGPV
PSTEKALANA GLDIGDIGLF EINEAFAVQV LSFLDHFGIA DDDPRVNRYG GAIAVGHPLA
SSGVRLMNQL ARQFQEDHSV RYGITAMCVG LGMGATVIWE NPHHADYSGA DRSDAVDSAS
TSTAGASA
//
