ID A0A0Q2XE22_MYCGO Unreviewed; 389 AA.
AC A0A0Q2XE22;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQH79476.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KQH79476.1};
GN ORFNames=AO501_11835 {ECO:0000313|EMBL:KQH79476.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH79476.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH79476.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH79476.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) 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:KQH79476.1}.
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DR EMBL; LKTM01000101; KQH79476.1; -; Genomic_DNA.
DR RefSeq; WP_055577684.1; NZ_LKTM01000101.1.
DR AlphaFoldDB; A0A0Q2XE22; -.
DR STRING; 1778.A9W97_04180; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000051677; Unassembled WGS sequence.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KQH79476.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051677};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQH79476.1}.
FT DOMAIN 8..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 267..388
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 389 AA; 41147 MW; 3AA438019ECA6467 CRC64;
MAGYSEAYVI DAVRTAVGKR GGGLAGVHPV DLGALGWRGL LDRVDVDPAA VDDVIAGCVD
AIGGQAGNIA RLSWLAAGYP EEVPGVTVDR QCGSSQQAIS FGAQAIMSGT ADLIVAGGMQ
NMSQIPISSA MTVGEQFGFT SPTNESKQWL HRYGDQEISQ FRGSEMIAEK WNLSREEMEQ
YSLNSHEKAF AAIRGGNFDN EILSVETETG AFRVDEGPRE SSLEKMAGLK TLVEGGRLTA
AMASQISDGA SAVLLASEQA VKDHGLTPRA RIHHISTRGA DPVFMLTGPI PATRYALEKT
GLSIDDIDTV EINEAFAPVV MAWLKEIKAD PERVNPNGGA IALGHPLGAT GAKLFTTMLN
TLERIGGRYG LQTMCEGGGT ANVTIIERL
//
