ID A0A0M2HAG4_9MICO Unreviewed; 394 AA.
AC A0A0M2HAG4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=RS82_01524 {ECO:0000313|EMBL:KJL43468.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL43468.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL43468.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL43468.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL43468.1}.
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DR EMBL; JYJA01000031; KJL43468.1; -; Genomic_DNA.
DR RefSeq; WP_045297967.1; NZ_JYJA01000031.1.
DR AlphaFoldDB; A0A0M2HAG4; -.
DR PATRIC; fig|69370.6.peg.1558; -.
DR OrthoDB; 3204099at2; -.
DR Proteomes; UP000034098; 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:KJL43468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KJL43468.1}.
FT DOMAIN 6..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 274..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 39981 MW; 6889BCC1D6547076 CRC64;
MNHDDVVIVA AARTPQGRLK GQLAPLTAVQ LGSAAIKGAL ERGGIPADAV DAVLVGQVLA
AGSGQNPARQ AAVGAGIGWD VHSSSVNKVC LSGLTAIIDG ARMLAVGDAT VVVAAGMESM
TRAPHLLMGS RDGWAYGSIE VLDHMAFDGL TDAYDRESMG ASTERHNERL EVTRQAQDAV
AARSHQRAAA AQAQGLFDAE IVPVEIPQRK GDPVVVTKDE GVRPETTVET LAGLRPAFAS
SGSITAGNSS QISDGASAVV LTTRSHADEN GWNVLAVVGA SGQVAGPDNS LHSQPARAIE
KALAKQGIAA SDLDIVEINE AFGAVVVRSQ AELGLSDDVV NPHGGGIAIG HPIGASGNRL
VVHAVHELVR RGGGTAAVAL CGGGGQGDAL ILTR
//
