ID A0A1I5EHF5_9ACTN Unreviewed; 1723 AA.
AC A0A1I5EHF5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SFO10949.1};
DE Flags: Fragment;
GN ORFNames=SAMN04487980_10632 {ECO:0000313|EMBL:SFO10949.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFO10949.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFO10949.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFO10949.1,
RC ECO:0000313|Proteomes:UP000198530};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; FOUV01000063; SFO10949.1; -; Genomic_DNA.
DR Proteomes; UP000198530; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
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; 2.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFO10949.1}.
FT DOMAIN 33..450
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 996..1071
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1085..1505
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 511..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1723
FT /evidence="ECO:0000313|EMBL:SFO10949.1"
SQ SEQUENCE 1723 AA; 179888 MW; 6021E8391C1FB7BC CRC64;
MANDDKVVDY LKRVTADLQR TRGRLRELEA SRREPVAIVA MACRFPGGVT TPEELWHLVA
EGRDAIGAFP ADRGWRTDGL ADAGARLEGG FLYGAGDFDA EFFGVSPREA LAMDPQQRLL
LETSWEAIER SGLDPDDLKG SDGGVFVGMT DQKYGPEDDD ALREVRGHIL TGTTSSIASG
RLAYFYGLEG PALTVDTACS SSLVALHLAI RALRARECSF ALVGGATVMA RPGLYEEFLL
QGGLAGDGRC KAFSDAADGT GWAEGAGVLV LERLSDALRA GHQVLAVVRG SAVNQDGASN
GLTAPNGPSQ QRVIRAALTD AGLSPAQVDA VEAHGTGTRL GDPVEAQALL ATYGQERELP
LYLGSLKSNI GHAQAVSGLG GVIKTVLAIR HGVLPRTLHV DAPTAEVDWS AGSVELLTEA
RAWPDTGRPR RAGVSSFGIS GTNAHVVLEQ APVGEAPVGE GPVQQAPVRE TTVDARSEEP
GGNAPVALLL SARTPEALRE QAARLQDHIG HAGNATPVDH ADHADHADHD GQVDDAAGVS
ISTSDADGSA PRGAAPAPRA VARALAARRP RFTHRAVVVG ADRTDLPAAL DALAQGTPDA
RVVRGAAAGA GPLAFLFTGQ GAQRVGMGRE LYAAHPVFTE AFDAVCARID PRLGRPLTDA
LASEELLGRT AYTQTALFAF EVALFRLLEH WGLAPDHLLG HSIGELAAAH AAGVLSLDDA
CTLVAARATL MDSLPEGGAM LAVEIAETDV PALLDAADAT GRLTVAAVNG PRATVLSGPA
DAVDATAALC AERGLRTRRL KVSHAFHSPL MEPMLDRFRA VAEGLTFHAP RIPLVSNVTG
LLATEEQLRS PDYWVRHVRE TVRFHDGVRL LGELGTTACL ELGPGGALSV LARDCLPDGT
AAFVPSLPHG HHEPTALLTA LGELHVRGVG VDWSAVLGTG GSTGQGGPED TLADLPTYPF
QRTRFWLPAI AGTGAPLLAA PPPAVTGAEP SARGRAFDVD LVRAVAAAVL GHPTLGAVPP
DRPFKDLGFD SLSAVRFRDR LAEETGLPLP TTLVFDHPTP EAVVAHLNGE HTGRSAAVRR
RAVMDEPLAV VGMACRYPGG VTTPEELWHL VAEGRDAVTA FPRDRGWDPT ALRRIDGGTP
TTGGFLHDAA EFDADFFGIS PREALAMDPQ QRLLLETSWE ALERTGIDPV SLRGSRTGVF
AGIAGSDYAG VLASTRETEG HVMTGTAGSV VSGRVSYVLG LEGPAVTVDT ACSSSLVALH
LAGQALRAGE CDLALAGGVT VMNTLGGFLE FARQGGLASD GRCKAFAESA DGTGWAEGAG
VLVLERLSDA RRHGRRVLAV VRGSAVNQDG ASNGLTAPNG PSQQRVIRDA LASAGLSPSE
VDAVEAHGTG TRLGDPIETQ AVLATYGQER ERERPLWLGS LKSNIGHSMA AAGVGGVIKT
VMALREGLLP RTLHIDEPTR QVDWSTDTVR LLTDAVPWPE TGRPRRAGVS SFGMSGTNAH
VILEHSPVDQ ALVGRDPVEP VPADQGGGHR RVRPWLLSAR TPDALRAQAA RLAAHLDRDD
GADATPAALG SALLRSRSLF EHRAVVLGTD RADLLTGVRA LADGTATAPK VITGTAAPTG
RGPVFVFPGQ GSQWAGMAVE LLEASPVFAA RMAECERALS VFVDWSLSEV LSDEGELARV
DVVQPVLWAV MVSLAEVWRS YGVEPAAVVG HSQGEIAAAV VAG
//
