ID A0A172UR69_9MYCO Unreviewed; 391 AA.
AC A0A172UR69;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=A7U43_21185 {ECO:0000313|EMBL:ANE81473.1};
OS Mycobacterium adipatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE81473.1, ECO:0000313|Proteomes:UP000077143};
RN [1] {ECO:0000313|EMBL:ANE81473.1, ECO:0000313|Proteomes:UP000077143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE81473.1,
RC ECO:0000313|Proteomes:UP000077143};
RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT sp. YC-RL4.";
RL Submitted (MAY-2016) 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; CP015596; ANE81473.1; -; Genomic_DNA.
DR RefSeq; WP_067999131.1; NZ_CP015596.1.
DR AlphaFoldDB; A0A172UR69; -.
DR STRING; 1682113.A7U43_21185; -.
DR KEGG; madi:A7U43_21185; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000077143; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000077143};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ANE81473.1}.
FT DOMAIN 5..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 86
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40622 MW; 2D16B748CA140B70 CRC64;
MPSPVIVGAA RTAIGRSFKG TLVNTPPEEL LVPVLAEVVR RAGLEPTAIN DLIIAESNYG
GGDLARYCAD ILGWHGVPGQ AVNRHCAGSL TAIGNASAHV ACGMERVVIG GGVQSLSMTP
LTNWRIPGPE LKFEERWMTP THVETPDAPM RDMSITVGWN TAQSAGITRE DMDAWAARSH
QRAVAAQDAG KFLDEIVPIK VTQPDGSVVE FSVDEHPRRG TTAEKLAELK VLHPEIDGFS
ITAGNSSGTN DAAAAVAVVA DDYAAAENLA VLATVKAWGS VGVAARDTGL GGVKVIGYVL
ERAGLKPSDV ALWEINEAFA SVPIAAVREY GIDEELVNFS GSGCSLGHPI SASGARMVTT
LIYELQRRGG GIGVAAMCAG GGQGGGLVIE V
//
