ID A0A1A3PZ54_9MYCO Unreviewed; 387 AA.
AC A0A1A3PZ54;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OBK39438.1};
GN ORFNames=A5658_24175 {ECO:0000313|EMBL:OBK39438.1};
OS Mycobacterium sp. 1245111.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK39438.1, ECO:0000313|Proteomes:UP000092232};
RN [1] {ECO:0000313|EMBL:OBK39438.1, ECO:0000313|Proteomes:UP000092232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245111.1 {ECO:0000313|EMBL:OBK39438.1,
RC ECO:0000313|Proteomes:UP000092232};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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:OBK39438.1}.
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DR EMBL; LZLV01000042; OBK39438.1; -; Genomic_DNA.
DR RefSeq; WP_067332985.1; NZ_LZLV01000042.1.
DR AlphaFoldDB; A0A1A3PZ54; -.
DR STRING; 1834073.A5658_24175; -.
DR OrthoDB; 3607666at2; -.
DR Proteomes; UP000092232; 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OBK39438.1}.
FT DOMAIN 5..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 264..386
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 387 AA; 40720 MW; EB090223B45751DD CRC64;
MGNPVIVEAT RSPIGKRAGW LSGLHATELL GATQKALVEK AGIDPGDVEQ VIGGCVTQYG
EQSNNITRVS WLVAGLPEHV GAMTVDCQCG SGQQANGLIA GLIAAGAIDV GIACGIEAMS
RVGLGANAGP DRGILRPASW DIDLPDQFTA AERIAKRRGI TREEIDQFGF DSQRKAKQAW
AEGRFDREIS GIQAPVLDEN KQPTSERHIV TKDQGLRDTT LEGLASLKPV IDGGIHTAGT
SSQISDGAAA VLWMDEDKAK ALGLKPRARI VSQALVGAEP YYHLDGPVQS TAKVLEKAGM
KMGDIDITEI NEAFASVVLS WARVHNPDMD KVNVNGGAIA LGHPVGSTGS RLITTALHEL
ERTDQTTALI TMCAGGALST GTIIERI
//
