ID V5X765_MYCNE Unreviewed; 432 AA.
AC V5X765;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AHC23623.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:AHC23623.1};
GN ORFNames=D174_03025 {ECO:0000313|EMBL:AHC23623.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC23623.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC23623.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC23623.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP006936; AHC23623.1; -; Genomic_DNA.
DR RefSeq; WP_023985150.1; NC_023036.2.
DR AlphaFoldDB; V5X765; -.
DR KEGG; mne:D174_03025; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_11; -.
DR Proteomes; UP000018763; 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; -; 1.
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; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:AHC23623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018763};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AHC23623.1}.
FT DOMAIN 9..277
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 287..431
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 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 432 AA; 45345 MW; 18432181997B446D CRC64;
MANTNSRRVA VLGGNRIPFV RSDGAYANAS NQDMFTAVLD GLADRFNLKG EKLDAVIGGA
VLKHSRDFNL MRESVLGSSL SPYTPAFDLQ QACGTGLQSA IAAADGIAMG RYEVAAAGGV
DTTSDAPIAF GDDLRGVLLS LRRAKSTADR LKLVGKLPAA LGVEIPTNGE PRTGLSMGEH
AAITAKQMGV KRVDQDELAA ASHRNMAAAY DRGFFDDLVT PFLGVYRDNN LRPDSSAEKL
ARLKPVFGVR NGDATMTAGN STPLTDGASV ALLSSEEWAA AHDIPVLAYF VDGETAAVDY
VNGSDGLLMA PTYAVPRLLA RNGLTLQDFD FYEIHEAFAS VVLATLAAWE SDDYCKNRLG
LDKALGSIDR AKLNVNGSSL AAGHPFAATG GRIVAQLAKQ LAEKKKETGQ PVRGLISICA
AGGQGVTAIL EA
//
