ID A0A370ATE0_9ACTN Unreviewed; 650 AA.
AC A0A370ATE0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RDG30934.1};
DE Flags: Fragment;
GN ORFNames=DVH02_33820 {ECO:0000313|EMBL:RDG30934.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG30934.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG30934.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG30934.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-2018) 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:RDG30934.1}.
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DR EMBL; QQNA01000419; RDG30934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370ATE0; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000253741; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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; 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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000253741}.
FT DOMAIN 1..351
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 323..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDG30934.1"
FT NON_TER 650
FT /evidence="ECO:0000313|EMBL:RDG30934.1"
SQ SEQUENCE 650 AA; 66462 MW; BB2C1455AC4F7FA2 CRC64;
FFGISPREAS VMDPQQRLLL TASWEALERA GIDPATLRGE QAGVFVGSSD QGYGAAAAAA
PDRVEGHMLT GGSGAVLSGR IAYTLGFEGP AVTIDTMCSS SLVALHLAVQ ALRQDECGIA
LAAGATVMAT PRNFVEFSRQ RGLAPDGRCK PFAAGADGTG WGEGVGVLML ERLSDARRLG
HPVLAVVRGS AVNQDGASNG LTAPNGPSQE RVIRAALANA RLTPDLVDVV EAHGTGTTLG
DPIEAQALLA TYGQGRDAQT PLWLGSVKSN IGHLQASSGV AGVIKMVLAM RHGILPKLLH
LDEPTSHVDW SSGAVELLTE NRDWPETGRP RRAGVSSFGG SGTNAHIVLE QAPASEPETE
PDPEDAPETS SVPAALPVFA PGATLPFVFS GRGADGLAAQ AARLTAFAGA SENAVRPRDL
AWSLAATRAA FENRAVALGT DHTDLTRAAV ALTSGAGDPA LVTGAFDVAP DGVVFVFPGQ
GAQWVGMGRE LWEVSPVFAA SMVACGEALA PFVGWSLEDV VRSGGGLVDV DVVQPVSWAV
MVSLAAVWRA VGVVPSVVVG HSQGEIAAAV VAGGLSLEDG ARVVALRSRA IRAIAGRGGM
VSVSLPLAEV EELLAGWVGR IDVAAVNGPG SVVVAGDADA LDELVARCEL
//