ID A0A2S8LDW4_9MYCO Unreviewed; 387 AA.
AC A0A2S8LDW4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Steroid 3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:PQP49695.1};
GN ORFNames=C6A82_09685 {ECO:0000313|EMBL:PQP49695.1};
OS Mycobacterium sp. ITM-2016-00318.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2099693 {ECO:0000313|EMBL:PQP49695.1};
RN [1] {ECO:0000313|EMBL:PQP49695.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITM-2016-00318 {ECO:0000313|EMBL:PQP49695.1};
RA Meehan C.J., Cogneau S., Rigouts L., Shojaei H., Azadi D.;
RT "Bioremediation-capable novel species from Iranian environmental samples:
RT Mycobacterium khaydaluicum sp. nov., Mycobacterium meyganicum sp. nov.,
RT Mycobacterium omidicum sp. nov., Mycobacterium seymaricum sp. nov.,
RT Mycobacterium austroafricanum subspecies dezhpoolicum subsp. nov.";
RL Submitted (FEB-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}.
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:PQP49695.1}.
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DR EMBL; PUTV01001264; PQP49695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8LDW4; -.
DR OrthoDB; 3607666at2; -.
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}.
FT DOMAIN 5..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 265..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; 40774 MW; 9445163E2A3FBE4C CRC64;
MGNPVIVEAT RSPIGKRNGW LSGLHPTELL GAVQRAVVEK AGIDAGEVEQ VIGGCVTQFA
AQSNNISRVA WLVAGLPEHV GATTVDCQCG SGQQANHLIA GLIAAGAIDV GVACGIEAMS
AIGLGANAGP DRSVLRPSSW DIDLPDQFTA AERIAKRRGI TRDDIDEWGF QSQARAKQAW
AEGRFDREIS PIEAPVLDEQ KQPTSERAFV TRDQGLRDTT KEGLASLKPV IDGGIHTAGT
SSQISDGAAA VLWMDEDKAK ALGLRPRARI ISQALVGAEP YYHLDGPVQS TTKVLEKAGM
KMGDIDITEI NEAFASVVLS WARVHNPDMD KVNVNGGAIA LGHPVGSTGS RLITTALHEL
ERTDQSTALV TMCAGGALST GTIIERI
//
