ID A0A176Q8Z9_9MICO Unreviewed; 399 AA.
AC A0A176Q8Z9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=AWH69_14905 {ECO:0000313|EMBL:OAB86186.1};
OS Janibacter melonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB86186.1, ECO:0000313|Proteomes:UP000076976};
RN [1] {ECO:0000313|EMBL:OAB86186.1, ECO:0000313|Proteomes:UP000076976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD11-4 {ECO:0000313|EMBL:OAB86186.1,
RC ECO:0000313|Proteomes:UP000076976};
RA Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL Submitted (JAN-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}.
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:OAB86186.1}.
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DR EMBL; LQZG01000005; OAB86186.1; -; Genomic_DNA.
DR RefSeq; WP_068277774.1; NZ_LQZG01000005.1.
DR AlphaFoldDB; A0A176Q8Z9; -.
DR STRING; 262209.AWH69_14905; -.
DR Proteomes; UP000076976; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000076976};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OAB86186.1}.
FT DOMAIN 8..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..395
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 399 AA; 40423 MW; 2F47D5570F1949F8 CRC64;
MSDRPVSVIV AGARTPMGRM SGSLKGFSGS DLGGFAIAGA LERSGVSPQD VDYVIMGQVL
TAGEGQIPAR QAAVKAGIPM TVPALTVNKV CLSGIDAIAL ADQLIRAGEF DVVVAGGQES
MTNAPHLLPK SRDGIKYGDA TLQDSMAYDG LYDVLTGQAM GSLTETGNSS GDQLSREEQD
AFAARSHQAA AKAWAEGRLA EEVVPVEVPQ RKGDPVVFAQ DEGIRADTTT ESLGRLRPAF
AKDGTITAGS ASQISDGACA VVVMSKAKAE ELGLDYLAEI GAHGVVAGPD SSLQAQPANA
IEAACAKEGI SPADLQLVEI NEAFAAVGIA STKQLGVDPE IVNVNGGAIA MGHPLGMSGA
RVVLTLAHEL KRRGGGVGAA ALCGGGGQGD ALVLRVPSA
//