ID V5XFB6_MYCNE Unreviewed; 393 AA.
AC V5XFB6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=D174_20090 {ECO:0000313|EMBL:AHC26712.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26712.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC26712.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26712.1,
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|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP006936; AHC26712.1; -; Genomic_DNA.
DR RefSeq; WP_019511566.1; NC_023036.2.
DR AlphaFoldDB; V5XFB6; -.
DR KEGG; mne:D174_20090; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_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; -; 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 ECO:0000313|EMBL:AHC26712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018763};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AHC26712.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40439 MW; 099B225BC0854FB8 CRC64;
MTTSVIVAGA RTPVGKLMGS LKDFSGSDLG AFAIKGALEK AGIDAGIVDY VIMGQVLTAG
AGQMPARQSA VAAGIGWDVP ALTINKMCLS GIDAIALADQ LIRAGEFEVV VAGGQESMSQ
APHLLPKSRE GFKYGDTTLV DHMAYDGLHD VFTDQPMGAL TEQRNDVDQF TRAEQDELAA
QSHQKAAAAW KDGVFADEVV PVQIPQRKGD PIEFAEDEGI RANTTAESLG GLRPAFRKDG
TITAGSASQI SDGAAAVVVM SKAKAEELGL EWLVEIGAHG VVAGPDSTLQ SQPANAIKKA
IAREGITVDQ LDVVEINEAF AAVSLASTKE LGIDPAKVNV NGGAIAIGHP IGASGARITL
HAALELARKG SGYAVAALCG AGGQGDALVL RRP
//