ID A0A448I310_MYCCI Unreviewed; 393 AA.
AC A0A448I310;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=NCTC10485_01315 {ECO:0000313|EMBL:VEG46869.1};
OS Mycolicibacterium chitae (Mycobacterium chitae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG46869.1, ECO:0000313|Proteomes:UP000282551};
RN [1] {ECO:0000313|EMBL:VEG46869.1, ECO:0000313|Proteomes:UP000282551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG46869.1,
RC ECO:0000313|Proteomes:UP000282551};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134355; VEG46869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448I310; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000282551; Chromosome 1.
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:VEG46869.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282551};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:VEG46869.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 210..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 40327 MW; 1603B893B049413A CRC64;
MTTSVIVAGA RTPIGKLSGS LKDFSGSDLG AIAIKGALEK GGVDPAAVQY VIMGQVLSAG
AGQMPARQAA VGAGIPWDVP SLSINKMCLS GIDAIALADQ LIRAGEFDVV VAGGQESMTQ
APHLLIDSRS GYKYGDVVVK DHLAYDGLHD VFTDQPMGAL TEQRNDEDKF TRAEQDEYAA
ASHQKAAAAW KDGVFADEVV SVSIPQRKGD PIEFSEDEGI RGNTTAESLG GLRPAFRKDG
TITAGSASQI SDGACAVVVM SKAKAQELGL DWLCEIGAHG VVAGPDSTLQ SQPANAIKKA
IAREGITVDQ LDVIEINEAF SAVSLASTKE LGVDPAKVNV NGGAIAVGHP IGMSGARIAL
HVALELKRRG SGYGVAALCG AGGQGDALVL RAG
//
