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Database: UniProt
Entry: A0A291GJJ1_9MICO
LinkDB: A0A291GJJ1_9MICO
Original site: A0A291GJJ1_9MICO 
ID   A0A291GJJ1_9MICO        Unreviewed;       406 AA.
AC   A0A291GJJ1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:ATG50519.1};
GN   ORFNames=CFK38_02510 {ECO:0000313|EMBL:ATG50519.1};
OS   Brachybacterium vulturis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=2017484 {ECO:0000313|EMBL:ATG50519.1, ECO:0000313|Proteomes:UP000218165};
RN   [1] {ECO:0000313|Proteomes:UP000218165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VM2412 {ECO:0000313|Proteomes:UP000218165};
RA   Tak E.J., Bae J.-W.;
RT   "Brachybacterium sp. VM2412.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP023563; ATG50519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GJJ1; -.
DR   KEGG; brz:CFK38_02510; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000218165; Chromosome.
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; 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:SF134; BETA-KETOACYL COA THIOLASE FADA3-RELATED; 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:ATG50519.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218165};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ATG50519.1}.
FT   DOMAIN          6..273
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..404
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   REGION          219..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        360
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   406 AA;  41641 MW;  27D012AE5E6CE584 CRC64;
     MSEAFLVGGA RTPVGRYGGA LSSVRPDDLA ALVVRAAVER AGIDPAAVDE VILGNANGAG
     EENRNVARMA WLLCGYPDAV PGITVNRLCA SGMSAILMAS QMIRAGDADL VVAGGVESMS
     RAPWVMEKPA QPFARPGAVV DTSIGWRFTN PAFLSGQCSR DGKATFSMPE TAEEVARRYR
     TSREDCDAFA ARSHQRALAA IDAGRFSAEI APVTVADRKG RESVVQDDEG PRPGSTPEVL
     AGLRPVVPGG SVVTAGNASS LNDGASAIVV ASEAAVDKFG LRPRARVLAG ASAGLAPEIM
     GMGPVPSTRK VLERTGRAVE DLAAVELNEA FASQSLASMR ELGLDPATVN NDGGAIALGH
     PLGSSGSRIA LTLLGRLERE ASPGDLGLAT MCVGVGQGSA MLVEAV
//
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