ID A0A1V9KIK4_9ACTN Unreviewed; 400 AA.
AC A0A1V9KIK4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Beta-ketoadipyl CoA thiolase {ECO:0000313|EMBL:OQQ19297.1};
GN ORFNames=B0675_21135 {ECO:0000313|EMBL:OQQ19297.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ19297.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ19297.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ19297.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ19297.1}.
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DR EMBL; MWFK01000001; OQQ19297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9KIK4; -.
DR STRING; 1955065.B0675_21135; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000192467; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; PS00098; THIOLASE_1; 1.
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:UP000192467};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..270
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..400
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 400 AA; 41691 MW; 7B12C27AB3A5DFB1 CRC64;
MKDVYIVDAV RTPIGRYGGS LAGVRPDDLA AHAIRALLAR TPGLDPARIE DVYVGNANGA
GEENRNVGRM AALLAGLPTS VPGVTVNRLC ASGLEAVVQA ARAIAVGDAS IVLAGGVESM
TRAPYVLPKS DRAFPAGHTE MYSTTLGWRM VNPRMDPQWT IPLGESAELI ADKHRITREQ
QDEFALTSHR KAEQARHKGL FDAEIAPLTL PARKGDPVVF DADECVRADA SLDAMARLKP
SFRTEDGTVT AGNASPLNDG AAALLLVDEE GLAATGREPL ARVRSTGVSA IDPQYFGLAP
VEAVTRALAK AGRRFDDLST LELNEAFAAQ VLGCLAEWPA FDPAILNPQG GAIALGHPLG
ASGARLAGTV AHQLARAGGG VGVATLCIGV GQGLALVLER
//
