ID M3DZ36_9ACTN Unreviewed; 389 AA.
AC M3DZ36;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=3-ketoacyl-CoA thiolase/acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EMF26892.1};
GN ORFNames=H114_21953 {ECO:0000313|EMBL:EMF26892.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF26892.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF26892.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF26892.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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:EMF26892.1}.
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DR EMBL; AOHP01000091; EMF26892.1; -; Genomic_DNA.
DR RefSeq; WP_006134348.1; NZ_AOHP01000091.1.
DR AlphaFoldDB; M3DZ36; -.
DR PATRIC; fig|1284664.3.peg.4406; -.
DR OrthoDB; 3761315at2; -.
DR Proteomes; UP000011732; 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 Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..257
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 91
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; 40867 MW; A98424FA53455DC2 CRC64;
MRDAVVVEAV RTPIGKGKPH GALAHVHPVE LLAHTLRTLV ERSGVDPELI DDVIGGTVDQ
VGEQAMNTTR YAALSAGLPE SVPATTVDRQ CGSSQQAVHF AAQGVISGAY DIAVACGVES
MSRVPMWSNV PEGKDPFGPG IAARHPEGLV PQGISAELIA AKWSITREQM DAFAVSSHRR
AAAAWDAGLF DAEVAPLEGV TRDECVRPDT DAEVLAGLRP AYHDPGFAER FPQIEWNVTA
GNASPVNDGA SAVLVMAGET AARLGLRPLA RLHSFAVTGS DPLLMLTGVV PATEKVLRRA
GLALDDIDLF EVNEAFSSVV LAWQQETGAD LDKVNVHGGA IALGHPLGAS GTRLTTTLVH
AMQERGARYA LQTMCEAGGL ANAVILERI
//