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Database: UniProt
Entry: Q9KIZ8
LinkDB: Q9KIZ8
Original site: Q9KIZ8 
ID   Q9KIZ8_SORCE            Unreviewed;      1832 AA.
AC   Q9KIZ8;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   19-JAN-2010, entry version 51.
DE   SubName: Full=EpoC;
GN   Name=epoC;
OS   Sorangium cellulosum (Polyangium cellulosum).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=56;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SMP44;
RX   MEDLINE=20115953; PubMed=10649995; DOI=10.1126/science.287.5453.640;
RA   Tang L., Shah S., Chung L., Carney J., Katz L., Khosla C., Julien B.;
RT   "Cloning and heterologous expression of the epothilone gene cluster.";
RL   Science 287:640-642(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SMP44;
RX   MEDLINE=20293058; PubMed=10831849; DOI=10.1016/S0378-1119(00)00149-9;
RA   Julien B., Shah S., Ziermann R., Goldman R., Katz L., Khosla C.;
RT   "Isolation and characterization of the epothilone biosynthetic gene
RT   cluster from Sorangium cellulosum.";
RL   Gene 249:153-160(2000).
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DR   EMBL; AF217189; AAF62882.1; -; Genomic_DNA.
DR   SMR; Q9KIZ8; 6-885, 1193-1694, 1438-1793.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR020842; PKS/FAS_KR.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_reg.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.366.10; Ac_transferase_reg; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 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   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine; Transferase.
SQ   SEQUENCE   1832 AA;  193146 MW;  C1EEDB8F4473C2D2 CRC64;
     MEEQESSAIA VIGMSGRFPG ARDLDEFWRN LRDGTEAVQR FSEQELAASG VDPALVLDPN
     YVRAGSVLED VDRFDAAFFG ISPREAELMD PQHRIFMECA WEALENAGYD PTAYEGSIGV
     YAGANMSSYL TSNLHEHPAM MRWPGWFQTL IGNDKDYLAT HVSYRLNLRG PSISVQTACS
     TSLVAVHLAC MSLLDRECDM ALAGGITVRI PHRAGYVYAE GGIFSPDGHC RAFDAKANGT
     IMGNGCGVVL LKPLDRALSD GDPVRAVILG SATNNDGARK IGFTAPSEVG QAQAIMEALA
     LAGVEARSIQ YIETHGTGTL LGDAIETAAL RRVFDRDAST RRSCAIGSVK TGIGHLESAA
     GIAGLIKTVL ALEHRQLPPS LNFESPNPSI DFASSPFYVN TSLKDWNTGS TPRRAGVSSF
     GIGGTNAHVV LEEAPAAKLP AAAPARSAEL FVVSAKSAAA LDAAAARLRD HLQAHQGLSL
     GDVAFSLATT RSPMEHRLAM AAPSREALRE GLDAAARGQT PPGAVRGRCS PGNVPKVVFV
     FPGQGSQWVG MGRQLLAEEP VFHAALSACD RAIQAEAGWS LLAELAADEG SSQIERIDVV
     QPVLFALAVA FAALWRSWGV GPDVVIGHSM GEVAAAHVAG ALSLEDAVAI ICRRSRLLRR
     ISGQGEMAVT ELSLAEAEAA LRGYEDRVSV AVSNSPRSTV LSGEPAAIGE VLSSLNAKGV
     FCRRVKVDVA SHSPQVDPLR EDLLAALGGL RPRAAAVPMR STVTGAMVAG PELGANYWMN
     NLRQPVRFAE VVQAQLQGGH GLFVEMSPHP ILTTSVEEMR RAAQRAGAAV GSLRRGQDER
     PAMLEALGAL WAQGYPVPWG RLFPAGGRRV PLPTYPWQRE RYWIEAPAKS AAGDRRGVRA
     GGHPLLGEMQ TLSTQTSTRL WETTLDLKRL PWLGDHRVQG AVVFPGAAYL EMAISSGAEA
     LGDGPLQITD VVLAEALAFA GDAAVLVQVV TTEQPSGRLQ FQIASRAPGA GHASFRVHAR
     GALLRVERTE VPAGLTLSAV RARLQASMPA AATYAELTEM GLQYGPAFQG IAELWRGEGE
     ALGRVRLPDA AGSAAEYRLH PALLDACFQV VGSLFAGGGE ATPWVPVEVG SLRLLQRPSG
     ELWCHARVVN HGRQTPDRQG ADFWVVDSSG AVVAEVSGLV AQRLPGGVRR REEDDWFLEL
     EWEPAAVGTA KVNAGRWLLL GGGGGLGAAL RSMLEAGGHA VVHAAESNTS AAGVRALLAK
     AFDGQAPTAV VHLGSLDGGG ELDPGLGAQG ALDAPRSADV SPDALDPALV RGCDSVLWTV
     QALAGMGFRD APRLWLLTRG AQAVGAGDVS VTQAPLLGLG RVIAMEHADL RCARVDLDPT
     RPDGELGALL AELLADDAEA EVALRGGERC VARIVRRQPE TRPRGRIESC VPTDVTIRAD
     STYLVTGGLG GLGLSVAGWL AERGAGHLVL VGRSGAASVE QRAAVAALEA RGARVTVAKA
     DVADRAQLER ILREVTTSGM PLRGVVHAAG ILDDGLLMQQ TPARFRKVMA PKVQGALHLH
     ALTREAPLSF FVLYASGVGL LGSPGQGNYA AANTFLDALA HHRRAQGLPA LSVDWGLFAE
     VGMAAAQEDR GARLVSRGMR SLTPDEGLSA LARLLESGRV QVGVMPVNPR LWVELYPAAA
     SSRMLSRLVT AHRASAGGPA GDGDLLRRLA AAEPSARSGL LEPLLRAQIS QVLRLPEGKI
     EVDAPLTSLG MNSLMGLELR NRIEAMLGIT VPATLLWTYP TVAALSGHLA REACEAAPVE
     SPHTTADSAV EIEEMSQDDL TQLIAAKFKA LT
//
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Ontology (5)   
   GO (5)   
Chemical substance (4)   
   KEGG COMPOUND (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (34)   
   InterPro (20)   
   Pfam (5)   
   PROSITE (3)   
   Blocks (6)   
Literature (2)   
   PubMed (2)   
All databases (46)   
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