ID A0A1Q4YP85_9PSEU Unreviewed; 2347 AA.
AC A0A1Q4YP85;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OKI36387.1};
GN ORFNames=A6A25_21820 {ECO:0000313|EMBL:OKI36387.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI36387.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI36387.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI36387.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:OKI36387.1}.
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DR EMBL; LWLC01000007; OKI36387.1; -; Genomic_DNA.
DR RefSeq; WP_073887654.1; NZ_LWLC01000007.1.
DR STRING; 1835005.A6A25_21820; -.
DR Proteomes; UP000186828; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase 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 GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186828};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2000..2078
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2347 AA; 249124 MW; 23BB7881848D56F3 CRC64;
MVPNPGGTTD AHDGEASTGR TFPLEPVALV GIGCRFPGGV EDPRGFWDLI ASGTDAVGDI
PPDRWRADAF HDADPSTPGR MTVRQGGFLR HPVDRFDAGF FGLPPREAAA LDPQQRLLLE
VAWEAFEDAG IPLATTAGRA VGAYIGGFTF DAATHQLSDA NRHLVGTATP TGVSMTMLAA
RLSYTFDWHG PSLTLDTACS SSLVAFHHAC AALSRGECDV AVAGGVNVMV NPVTTILMSK
GQFLSPDGRC KSFDHRANGY ARAEGAAVVV LKSLAAAERD GDRVYAVVRG TAVNQDGRTP
GITVPSARAQ REVIRQACRS GGVEPASVGY YEAHGTGTAV GDPIEATAIG EVLGGSDRTH
WIGSVKSNIG HSEAAAGVAG VIKAALCLER GLIPPNLHFE RPNPRIPFDR LPLRVPTEVV
PFPVFPGPRR AGVNSFGFGG TNAHAILEQA PPAPAATDEE GDDGRPHVLP LSARSPEALR
ALAARYAELL ARPDAPALRR ISRAASRQRD HHPVRASVVA VDAAGAVERL RELEPAPRRA
PRGGVAFVYT GMGPQWWGMG RELLTTEPRF AEVVAECDAV LARFGLSIGE ELLRDEEDSR
LAETLYAQVA NFVVQAGLTA LWRAWGIEPS VVVGHSVGEV AAAYAAGVYS LQDALTVAFH
RAHLQSGLAG RGAMVAVDLT ADDVRPHLVD GVEVAAVNSA TATTLAGDQD AVEEVTRRLR
AAGASVKPLR VEVAYHSRHM DVVREPLLAA LHGIEPREAR VPLVSTVTGD RVTGAELDAV
YWWENVRRPV EFAAALRRVL SSAPGAVVEI GPHPVLAAAI DEGLSGHGDD VVRLASLRRD
RPQRQQVLEA LGALYAAGVD PDWEGVHSGP REHLDLPRYP WQRERHWVES SAAREARLGG
DGPRLAGRAV SAATPTRDVE LSESEFPYLA DHRIGDTVIF PGSGYLEAAL ALFPDDEFCF
FEDVVFQRPL ALGARSVTTL RVSHDPVHHL VTLHSRAQGD DAGWTPHARM RRPDVVRPRA
PRRWSETLEQ STRSLPEVGR DEVYALLDRS DLTYGPAFRG VERLWWREAT GEVFAEIRVD
AVDATGHRLH PALLDAALQA VIAGSLRLSG EEGTTYVPAR IAEFRFHRSP GRTLWLHGRD
RGATAPGRLE CDLTLITDDG EVVAEVIGLR AQRLVQDGGP TRPEGLHYEH TWRAEPLERT
GGAEGRWVVI GSSPVCAELA AELTARGGDV VRTSPEDETW LDVVRDATGG PCRGVVHVNG
PDRDDPAACA SVAAPLRLVQ TLADAVPLFL VTSGAQSATA DDHTVDPFAA ALWGFGRVVG
AERPDLRCRL VDVTPETGAG ALVDELTHAG LDEVVLRGAA RYVRRLERAG DRSPLHHVTT
RAGATPVRLR ANGSGVDGLG FAATGRRAPG PTEVEVEVSF VGLNFKDVLK VTGLLTPEAV
EGSLSRDALG LECSGTVVRV GEAVADLRPG DEVFVHGADL FASHVTVDAV RAVRKPSTLS
LARAASLLPV VTAHQALVRL ARVRPGERVL VHSAAGGVGL AAVRIASRLG AEVYATASSD
ERREFLRGEG VAGVSDSRST AFADDVLRWT GGEGVDVVVN SLSGELLRKS LGLLRPFGRF
VELGKVDIAA DHALGLAPFH RALSFHAFDY DRMMLLDPEL VRASMLDVVA LHEDGAIDPL
PVTEVPAGRV DAAFRAMTRA DHVGKVVVRV AGEPVAVPAA SVPGSPIRSD GTYLVTGGLG
GLGLAVAGWL ADQGARHLVL VGRRGIVTAD AERSVAELTG RGVEVRVERV DVADRAAVER
TFALLREQLP PVRGVVHAAA DFDDVVLADT DADRLITATR PKADGAWHLH LATQADELDF
FVLFSSVAAQ LGAAAAGAYA TANEFLNALA RHRRLKGLPA TAVGWGMVDS VGVAVRRDGA
VGDALRRNGH VGMSPARLVA ELEALLRTRP VELSVADVDW TRWARANPQL ARLPRYESLV
PAEAADGTGH ASVTQRLRDA SPAERLTLLS ELVTPLLQRT TGLTEEQLAD GQAVDIDSLV
AVELRVGLQN ALGVSVPAVK LQRNLTVSGL AGLLAEELDR APGTPSRPAE AITAHEFTSA
DGLVVHGHLS VPDGPGPHPA VVVCTAGEGG ALDDQGRYAR ISEHAPLLAA GFAVFTVDQR
GAPGHGAEYR ASADMGGRDI DDVVAAARHL AGLPGIDPAR VSVLGTSRGA YSALLALADE
PSLWHRAVLL MGLYDPTALV DAERSRPGTL LPRRVGADEV AAYFADPARQ PPARLGDVGT
PLLLVHGDAD DVVPVTQAVD LVERARRLDL PARLVTVPGL GHDHDHADEA WTTLWPRVAD
FLGEASR
//
