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Database: UniProt
Entry: A0A3G8JNC7_9ACTN
LinkDB: A0A3G8JNC7_9ACTN
Original site: A0A3G8JNC7_9ACTN 
ID   A0A3G8JNC7_9ACTN        Unreviewed;       412 AA.
AC   A0A3G8JNC7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   Name=thlA_1 {ECO:0000313|EMBL:AZG45680.1};
GN   ORFNames=D7316_02280 {ECO:0000313|EMBL:AZG45680.1};
OS   Gordonia insulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG45680.1, ECO:0000313|Proteomes:UP000271469};
RN   [1] {ECO:0000313|EMBL:AZG45680.1, ECO:0000313|Proteomes:UP000271469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG45680.1,
RC   ECO:0000313|Proteomes:UP000271469};
RA   Kim Y.S., Kim S.B.;
RT   "Gordonia insulae sp. nov., isolated from an island soil.";
RL   Submitted (NOV-2018) 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; CP033972; AZG45680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8JNC7; -.
DR   KEGG; gom:D7316_02280; -.
DR   Proteomes; UP000271469; Chromosome.
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; IPR020617; Thiolase_C.
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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:AZG45680.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271469};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AZG45680.1}.
FT   DOMAIN          9..272
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..409
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        93
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        367
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   412 AA;  43045 MW;  BE27E9ACDEC296E4 CRC64;
     MKDTVLRDVV ICEPVRTPIG RYGGMFKGVT AVDLGVTALR GLLDRTGLAP ELVDDVVLGH
     CNGNSEAPAI GRVVALDAGL PITVGGMHID RRCGSGLQAV IQAAFQVAAG DNDVVIAGGT
     ESMSNASFYS VDMRWGGART GIAMHDSLVR ARSTAGGKNY PVPGGMIETA ENLRKEYEIS
     RAEQDELAVE SHLRAVRAQK DGILAEEIIP VTVRGRGGDQ IIDTDEHPRP DVSVQSLAKL
     KPIMGTTDPD ATVTAGNASG QNDAAAMCIV TTPDVAQQHG LRPLVRLVSW AVAGVAPRTM
     GIGPVPATEK ALAKAGLTLT DIDVIELNEA FAAQALAVTR EWGFGRFGAG GDFDRTNVHG
     SGISLGHPVG ATGVRMLASL ARELRRRDAR YGLETMCIGG GQGLAAVFEN VG
//
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