ID A0A372G0Q6_9ACTN Unreviewed; 383 AA.
AC A0A372G0Q6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Steroid 3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:RFS46622.1};
GN ORFNames=D0Q02_10430 {ECO:0000313|EMBL:RFS46622.1};
OS Micromonospora craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS46622.1, ECO:0000313|Proteomes:UP000262621};
RN [1] {ECO:0000313|EMBL:RFS46622.1, ECO:0000313|Proteomes:UP000262621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63014 {ECO:0000313|EMBL:RFS46622.1,
RC ECO:0000313|Proteomes:UP000262621};
RA Li L., Lin H.W.;
RT "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT South China Sea.";
RL Submitted (AUG-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:RFS46622.1}.
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DR EMBL; QVFU01000008; RFS46622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372G0Q6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000262621; 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; 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; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000262621};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 261..382
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 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 383 AA; 39869 MW; 52F255253B8E84E8 CRC64;
MAEAVIVAAA RTPIGRRDGW LRGLKAVELL RTVQREVLDR AGLPASAVDQ IIGGCVTQVG
EQSLNVTRNA WLSTGLDPEV ACTTVDVSCG SAQQANHLIA ALISAGAIDV GIACGVESMS
RVPVGTNLYQ GPGHYKTDDY PWDDPPKAQF GGAERIAAKY GVDRAGADAY GLRSQRRAAA
AWAQGRFDTE VVAVRAPTPG GGTVEVTRDQ GLRESTPDGL AGLKPTVEGG VHTAGTTSQI
SDGAAAILWM SAERAAALGL RPRARLLHQV VTGSDPALLL EGPVVATRKI LDRAGMRLSD
IDVAEVNEAF AAVVLAWMAS HDADPERVNV NGGAIALGHP LGASGTRLLV SALHELERTD
RELALVTMCC GGALGTASIL QRM
//
