ID A0A2M8LXZ7_9ACTN Unreviewed; 855 AA.
AC A0A2M8LXZ7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:PJE96848.1};
DE Flags: Fragment;
GN ORFNames=CUT44_15765 {ECO:0000313|EMBL:PJE96848.1};
OS Streptomyces carminius.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2665496 {ECO:0000313|EMBL:PJE96848.1, ECO:0000313|Proteomes:UP000230407};
RN [1] {ECO:0000313|EMBL:PJE96848.1, ECO:0000313|Proteomes:UP000230407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM SA0054 {ECO:0000313|EMBL:PJE96848.1,
RC ECO:0000313|Proteomes:UP000230407};
RA Wang Y., Luo X., Wan C., Zhang L.;
RT "Streptomyces carmine sp. nov., a novel actinomycete isolated from Sophora
RT alopecuroides in Xinjiang, China.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:PJE96848.1}.
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DR EMBL; PGGW01000055; PJE96848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8LXZ7; -.
DR Proteomes; UP000230407; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000230407};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 35..461
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 460..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PJE96848.1"
FT NON_TER 855
FT /evidence="ECO:0000313|EMBL:PJE96848.1"
SQ SEQUENCE 855 AA; 91497 MW; 70B23F527729FD46 CRC64;
FDCPTPRAVA RFVLDELAGG AAEQAPVAAA VRTDDDPVVI VGMACRLPGG IASPEDLWKL
LEAGGEALSD FPTDRGWDID GIYDPEPGLP GKTYVRRGGF LEDAGGFDAA FFRISPREAL
AMDPQHRVFL ETSWEVFERA GVDVTALRGS RTGVFAGGFH TGYTVGADLI GEGVDGYTSH
NNLPSVLSGR VSYTFGFEGP AVTVDTACSS SLVALHLAVQ SLRSGESDLA LAGGVAVMPR
PSTFVEFSRQ RGLAADGRCK AFAAAADGTG WSEGVAVLLL ERLSDARRNG HTILATVRGT
ATNQDGASNG LTAPNGPSQQ RVIHQALANA NLTTTDIDAV EAHGTGTTLG DPIEAQALIN
TYGQHRNPDH PLWLGSLKSN IGHTQAAAGI AGVIKSVLAI HHATLPRTLH IDAPTPHVDW
TAGNVRLLTE TQPWPHTGHP RRIGISAFGV SGTNAHAIIE QPPTPETPDT ADTPPPTHDT
PVPWILSART PTALTELGRR LLDHLDHHPH LTPHQIATQL HHRARLDHRA VITGTDRDQM
LRALTALTHN TTDPDLTTGT PQNTGKTVFV FPGQGTQWAG MGARLLDTSP TFTDAITACD
TALAPYQDWT VTDVIRQTDN APTLDRVDVV QPVSFAVMVS LARLWQHHGI HPDAVIGHSQ
GEIAAATIAG ALTLDDAARI VALRSQAIAR HLAGHGAMLS IPLSLHDTRT WTDPHRDHID
IATVNGPTST VVAGHPTTID TLHTDLTNAD IRARKIPVDY ASHTSHVERI HNELTHLLTD
ITPHTPTTPM YSTTDRTWIT GPTLTGDYWY RNLRQTVHFH TGTTTLADTG HHTFIEVSAH
PVLTMAIEDT LQDHP
//
