ID M3D487_9ACTN Unreviewed; 3369 AA.
AC M3D487;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EMF31188.1};
GN ORFNames=H114_00010 {ECO:0000313|EMBL:EMF31188.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF31188.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF31188.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF31188.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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:EMF31188.1}.
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DR EMBL; AOHP01000001; EMF31188.1; -; Genomic_DNA.
DR RefSeq; WP_006129568.1; NZ_AOHP01000001.1.
DR PATRIC; fig|1284664.3.peg.2; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000011732; 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; cd08952; KR_1_SDR_x; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 1.20.5.1140; Docking domain of the erythromycin polyketide synthase (DEBS); 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR041618; PKS_DE.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1682..1757
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1774..2190
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3208..3283
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 462..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2188..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3369 AA; 349089 MW; 77AA696B542A29C9 CRC64;
MADDDKYVEY LKRVTGELRQ TRRRLREVED RAREPIAVVA MSCRFPGDVR GPEDLWRLVD
EGGDAIGALP ADRGWDIEDR YDPDPGNPGT FSTREGGFLG DAASFDAGFF GMSPREALAT
DPQQRLLLEA SWELLERAGI RPQTLRGSAT GVFVGAATSG YGQGPVEVPE DVHGLMLAGN
ATSVASGRIS YVLGLEGPTV TVDTACSSSL VALHWAVQAL RNGECDLAMA GGVAVMATPG
LLFEFSRQRG LAPDGRCKAF ADGADGTGWS EGVGLLLVER LSDARRNGHP VLAVVRGSAV
NSDGASNGLT APNGPAQQRV IEQALASAGL TAADVDAVEA HGTGTTLGDP IEAQALLATY
GQNRPADRPL LLGSLKSNLG HTQAAAGVAG VIKTVMALQH GRLPRTLHVD RPSTHVDWDA
GHVRLLTEPA DWPATGDRPR RAAVSSFGIS GTNAHVILEA APEPEPEPES EATDTPAAGT
TAAGATAAPA RPLPLAPWFV SARSAEALRG QAARLLKHVA DHPDDDPHDT VRALVTTRQT
FEHRAAVLAP DTAAARDALR ALADGEEHPA LVTGRTLRGA TAFLFPGQGA QRPGMGRDLY
AAFPAFARAY DEVCAHLDPE LGLSLKDTVL HSGDEEALRA TGLAQPALFA FEVALFRLLE
SWGVTPKYLL GHSLGELTAA HVAGVWSLAD ACRLVAARGR LLQALPEGGA MISVEAAEDE
VTPLLAAHGD AVSVAAVNGP RATVLSGDTA AVEAVAAELG ARGRTTRRLR VSHAFHSARM
DGALEEFRRV AAGVTARPPR ITVVSDLTGS PATADELASA DYWVRHVRHT VRFADGVDGL
VQRGVTRFLE LGPDATLTAL ARTCLPEDTT ERICLPLQRK DRPEPATLLA AVAGAHAHGV
PVDHDRLLGA PAPGAPRIEL PTYAFTRERY WLRPAASTGD VTGAGLAGTG HPLLGAVVRV
ADEDRVLLTG RLSTRAQAWL ADHTVAGTVL LPGTAFVELV LRAGDEVGCG LLDELTLEAP
LVLPDGHGVQ LQIVLGAPDD AGRRTVTVHA RPDADDDTPW TRHATAVLAP AAAARPGDTL
TAWPPAGATP VPLDGFYDAL ADQGYQYGPV FQGLRAAWRD GDVRYAEVSL PEDEHRDAAR
FGLHPALLDA ALHAQLTGTD EDGGQDGRRG GVGLPFAFGG VTLHAVGATT LRVRLERNAG
GAVTLHVADG TGQPVATVDS LVSRPLSDGA TGPARPADGA LYTVRWTPAD LPRTPAADRP
EDHGSTPAVL TFSSEPGETP ASVAARALDA LRTRLADDPT GDTPVVVVTR GAVATGGEED
VPDLPAAAVW GLVRSAQTEN PGRIVLADLD DTDASRAALD AAIASGAPQL ALREGRLLVP
SLTRAALSGA DRPAAWDPDG TVLVTGGTGA LGALVARHLV TTHGVRSLLL LSRSGPDAPG
AADLTAELTA HGAAVRVEAC DAADPEALAA ALAAVPAEHP LRAVVHTAGV LDDGVLGSLT
PDRLATVLRA KADSALALHH ATRDADLTAF VLFSSAAGLL GGAGQANYAA ANTVLDALAH
HRRAQGLPAV SLAWTLWDHD GGMTGGLDAD AVRRIAASGL PALDPAQALR LLDEALAADE
ALLAPLRTEP AALRAAATAG RLPALLHGLV PTPARRTARA ADAGSSELGR RLAALTETEQ
ERLLLDVVRR HAAVALGHGS AGAVDGEQSF KDLGFDSLTS VDLRNRLNAE TGLRLPATLV
FDHPRPSALA RHLRGELAGG TETARTAAVA ADDDDPVVIV SMACRYPGGV TSPEELWRFV
SEGGDAIGAF PADRGWDLDR LPGLQAGFLH DATHFDAALF GISPREALAM DPQQRLLLET
SWEVFERAGL DPLAQRGGRT GVYVGAMGSG YASGLADIPE GMEGYIGLGV SGSVISGRVA
YTFGLEGPTM TVDTACSSAL VALHLAAHAL RQGECAMALA GGVTVMATPG TYTEFTAQNG
LAADGRCKAF AASADGTSFS EGVGMLLLER LSDARRNGHP VLAVVRGSAT NQDGASNGLT
APSGPSQQRV IRAALDSAGL APADVDAVEA HGTGTTLGDP IEAQALIATY GQDRPDDRPL
WLGSAKSNFG HTQAAAGAAG VIKMVMAMHH GELPRTLHVD EPSPHIDWSA GAVRLLTESR
PWSAPDGRPR RAGVSSFGIS GSNAHVVLEE PPAPTPAPER EAAAGTPRAY PVSGHTPDAL
RAQAARLRAH LLTAGHDPRD LAHTLATARP ALAHRAVVVA EDHEELLAGL TALATGDQAG
HVVTGHADGG RLAVLFSGQG AQRPGMGRDL YAAHPVFADT FDAVCAELDR HLDGPPLREV
MFAAEGSAHA ELLDRTAWTQ AALFAFGTAA HALTSSWGVR PDVLAGHSVG ELTAAHAAGV
LDLADACALV AARGRLMQAL PEGGAMTAIE ATEAEVLPYL EDRADRIAVA AVNGPASVVV
SGAEDDVAAV AGEFTARGRR TRRLRVSHAF HSPLMDAMLE DFRKVAERVR YAPPAVPVVS
NLTGALGTGE DLRTPDYWVR HVREAVRFAD GVRTLRDEGV TLCLELGPDT TLTPLVRDGA
GDPDAVTAVS LLHRDLPEPR AALLAAAALH THGRADLPPA PADARPVALP TYAFQRERYW
LETSARPAAP TADGAFWELV EAADPAALAE RLDVDADAPL STVLPALAAW RGTDRRQREE
RRWEHRVTWR PAADGATAAL TGIWLLAVPE DLDGGPWASS VAEALTAHGA RVRVLPVDCA
RADRAGLAAA YDTAREDGPA LAGVLSLLAA DTRPLPGHGA VPAGLAATTA LVQALADRAT
GPDTTRLWAV TAGAAGVLGH EAPAAPEQAA VWGLGRTAAL EHPQLWGGLV DLPAGTLAAV
APDVARRLCA VLAGGTGEDQ TAVRPDGTFL RRLEHVPADA SAGTPADWTG TVLLTGATGA
LGLRTAAWLA ERGATRIVAV SRSGAGSPGA ARLKEALDGT GAELVLAACD AADRDALAAL
LAEHPVDAVV HTAGVLDDRL LDAMDADALE TVLRPKLAAA RNLHDLTRDR DLTAFVLYSS
VSGTLGTIGQ ANYAAANAYL DALAEQRRAA GLAATSLAWG PWAGGGMATR DAGTENRMRR
GGIQPLDPDR AVEALGRATA RTDAVLTVAD IDWARFAPGF TTSRPSPLLA ELPEVRELSD
TGPRGAAADA GQDLRARLAG QTPAERDRTL ITLVRTEAAA VLGHASTDRV GAAQAFNALG
FDSLTAVELR NRIGAATGLA LPATLLFDHP DATALAGYLR GRLTEDTDGG GAVLAELDRL
EAALSALAAD DARRDRIGAR LQSLLGRLGG GTAGAAPATA TGDGDIAGRL ESAAADELFD
FIENDLGIS
//
