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Database: UniProt
Entry: Q27W60_STRVO
LinkDB: Q27W60_STRVO
Original site: Q27W60_STRVO 
ID   Q27W60_STRVO            Unreviewed;      1942 AA.
AC   Q27W60;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=NigAIX {ECO:0000313|EMBL:ABC84469.1};
OS   Streptomyces violaceusniger.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=68280 {ECO:0000313|EMBL:ABC84469.1};
RN   [1] {ECO:0000313|EMBL:ABC84469.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 4137 {ECO:0000313|EMBL:ABC84469.1};
RX   PubMed=17584617; DOI=10.1016/j.chembiol.2007.05.011;
RA   Harvey B.M., Mironenko T., Sun Y., Hong H., Deng Z., Leadlay P.F.,
RA   Weissman K.J., Haydock S.F.;
RT   "Insights into polyether biosynthesis from analysis of the nigericin
RT   biosynthetic gene cluster in Streptomyces sp. DSM4137.";
RL   Chem. Biol. 14:703-714(2007).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; DQ354110; ABC84469.1; -; Genomic_DNA.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; 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; 1.
DR   Pfam; PF08990; Docking; 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; 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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
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}.
FT   DOMAIN          33..459
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1766..1848
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1370..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1465..1479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1942 AA;  201709 MW;  63561AF5F94BF8D2 CRC64;
     MTDDEKLRSY LKRATADLRL ARRQLREVED RAREPIAIIG IACHFPGDVA TPEDLWRVVD
     EGVDVISSFP EDRGWDLDSL YDPDPEHAGT SSAREGGFLR DVADFDAEFF GISPREAAAM
     DPQQRLLLET AWEAFERAGL TREALNGSRT GVFAGVDSYH YLSLIGQTTG DSAGYVATGN
     LGSVVSGRVS YSFGLEGPAV TVDTACSSSL VATHLAVQAL RQDECSLALA GGVTVMATPG
     GFTEFSRQRA LSPDGRCKAF AAAADGTGFS EGVGLVLLER LSDARRNGHR VLAVIRGSAV
     NQDGASNGLT APNGPSQQRV IRQALANAGL SPSEVDAVEA HGTGTTLGDP IEAQALLATY
     GQDRPEGRPL WLGSIKSNIG HTQAAAGVAS VIKMVQALRH EVLPVSLHID APTPHVDWGA
     GEVRLLSEPV EWAANEQPRR AGVSSFGISG TNAHLILEQA PAQPVEAARA PDSSRGGVPA
     GGVVPWVVSG RGAKALRGQA RALAERVATD PDASPAEVGW SLISTRSVFD HRAVIVGEHR
     DELLAGLNAL ATGDTHPTLT EPTTTGPGAG GMGPVLVFPG QGSQWLGMGA GLLDTSPVFA
     TRIAECEHAL TPHVDWSLTE VLRGGVNAAD LARVDVVQPV LWAVMISLAA VWDHHGLTPT
     AVVGHSQGEI AAACVAGALS LDEGARIVAL RAHALRRLAG HGAMASLTTS QTHTEELLTN
     LGEQADAVGV AAVNGPGSVV ISGPPEQVTH AITACEQAGH RARLIDVDYA SHSAQVDEIA
     EELNQLLAGV KPVSAQVAFY STVTGARMDT SGLDTAYWIK NLRERVRFAD AVRALLHDGH
     RVFIEASTHP VLTIGMQESI EEARVDAVTI PTLRRDHGGP DQLARSVARA FTAGLSVDWT
     RWFPTDPAPR TIDLPTYAFQ RERYWLDGEG GPGGDPAGLG LTAAGHPLLG AAVELADGTT
     HVLTGRISAR SHPWLAEHVV AGAVLAPGAV LVEWALRAAD AVGCGGVEEL ALQVPLALPE
     SGGLRVQVVV GAAAEDGRRE VRMYSSPDHP NSLDPGLDSG ADTGWVCHAV GVLAPAAEAP
     APVEGLGGAW PPPGAEPLDV GAFYEQVLAA GYGYGPAYQG LKAAWRQGGD VLAEVALPDA
     AGGRDGYGIH PALLDAALHP SLLMDRPEGQ EDDGQVWLPF AWNGVSLWAT EAATVRVRLS
     RDEERQSLRL TVADTVGAPV LTVDSLVTRP AAADQLCSAA AARAVDGLFT LDWMAVPAPA
     TAPSPASVVG EGSWVVLGED RLGLAEPVAA GLGADATVSH PDLEALIAAV DAGEPAPAVV
     LTHPYTAEGG HGDGLGAVEE LLGLVRSWLR RPALADARLV VVTRGAVAAG RAGDATDDAD
     DTALDPSGVD PSGAGAWGLI RSAQSENPGR FVLLDLDEGH EGRAGLVEAV VRAVESHEPQ
     MAVRDGRVLV PRMVRAMAAP GPTTDDRGES TTGLDENTTG LDGGATGLDT DGTVLITGGT
     GTLGTLVAEH LVRAWGVRHL LLVSRSGPEA AGAGELTAAL TELGAEVRIA AVDVTDPDAV
     AALVAGVDSA HPLTGVVHAA GVLDDGVLTT QTPERLARVW RPKATAAAHL HAATAELPLS
     LFVMFSSTAG TLGASGQSNY AAANAYCDAL AARRHALGLP GLSVAWGLWA DASGMTGHLG
     EADRARMTRS GIGAMSSERA LGLLDAAMRH GHHHLIAIDL DVRALTGRPA LTLPAPLRAL
     AGGGTARRTA ATARPHTDWA GHLAALPLEE QRRTLLNLVL SHAAAALGHS DPGRIQTERG
     FLELGFDSLT AIELRNRLTA VTGLRLATTL IFDHPNPAAL AAHLHSELAP EDADPLAPML
     GEIDRMESAL LSVAQDETAH EALLERLRTT LSKLGALHGG GTEEGPAAGR IQDATADEIF
     QFIDEDLGRS ESNGEHAHGG TR
//
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