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Database: UniProt
Entry: Q9KJ00
LinkDB: Q9KJ00
Original site: Q9KJ00 
ID   Q9KJ00_SORCE            Unreviewed;      1421 AA.
AC   Q9KJ00;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   19-JAN-2010, entry version 50.
DE   SubName: Full=EpoA;
GN   Name=epoA;
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; AAF62880.1; -; Genomic_DNA.
DR   HSSP; P96202; 1PQW.
DR   SMR; Q9KJ00; 4-890, 952-1273, 1293-1385.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; 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; IPR013154; ADH_GroES-like.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR011032; GroES-like.
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; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_reg.
DR   InterPro; IPR020843; PKS_ER.
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; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine; Transferase.
SQ   SEQUENCE   1421 AA;  148745 MW;  3D055DDBF686E2C5 CRC64;
     MADRPIERAA EDPIAIVGAG CRLPGGVIDL SGFWTLLEGS RDTVGQVPAE RWDAAAWFDP
     DLDAPGKTPV TRASFLSDVA CFDASFFGIS PREALRMDPA HRLLLEVCWE ALENAAIAPS
     ALVGTETGVF IGIGPSEYEA ALPRATASAE IDAHGGLGTM PSVGAGRISY VLGLRGPCVA
     VDTAYSSSLV AVHLACQSLR SGECSTALAG GVSLMLSPST LVWLSKTRAL ATDGRCKAFS
     AEADGFGRGE GCAVVVLKRL SGARADGDRI LAVIRGSAIN HDGASSGLTV PNGSSQEIVL
     KRALADAGCA ASSVGYVEAH GTGTTLGDPI EIQALNAVYG LGRDVATPLL IGSVKTNLGH
     PEYASGITGL LKVVLSLQHG QIPAHLHAQA LNPRISWGDL RLTVTRARTP WPDWNTPRRA
     GVSSFGMSGT NAHVVLEEAP AATCTPPAPE RPAELLVLSA RTAAALDAHA ARLRDHLETY
     PSQCLGDVAF SLATTRSAME HRLAVAATSS EGLRAALDAA AQGQTPPGVV RGIADSSRGK
     LAFLFTGQGA QTLGMGRGLY DVWPAFREAF DLCVRLFNQE LDRPLREVMW AEPASVDAAL
     LDQTAFTQPA LFTFEYALAA LWRSWGVEPE LVAGHSIGEL VAACVAGVFS LEDAVFLVAA
     RGRLMQALPA GGAMVSIAAP EADVAAAVAP HAASVSIAAV NGPDQVVIAG AGQPVHAIAA
     AMAARGARTK ALHVSHAFHS PLMAPMLEAF GRVAESVSYR RPSIVLVSNL SGKAGTDEVS
     SPGYWVRHAR EVVRFADGVK ALHAAGAGTF VEVGPKSTLL GLVPACLPDA RPALLASSRA
     GRDEPATVLE ALGGLWAVGG LVSWAGLFPS GGRRVPLPTY PWQRERYWID TKADDAARGD
     RRAPGAGHDE VEKGGAVRGG DRRSARLDHP PPESGRREKV EAAGDRPFRL EIDEPGVLDR
     LVLRVTERRA PGLGEVEIAV DAAGLSFNDV QLALGMVPDD LPGKPNPPLL LGGECAGRIV
     AVGEGVNGLV VGQPVIALSA GAFATHVTTS AALVLPRPQA LSATEAAAMP VAYLTAWYAL
     DGIARLQPGE RVLIHAATGG VGLAAVQWAQ HVGAEVHATA GTPEKRAYLE SLGVRYVSDS
     RSDRFVADVR AWTGGEGVDV VLNSLSGELI DKSFNLLRSH GRFVELGKRD CYADNQLGLR
     PFLRNLSFSL VDLRGMMLER PARVRALFEE LLGLIAAGVF TPPPIATLPI ARVADAFRSM
     AQAQHLGKLV LTLGDPEVQI RIPTHAGAGP STGDRDLLDR LASAAPAARA AALEAFLRTQ
     VSQVLRTPEI KVGAEALFTR LGMDSLMAVE LRNRIEASLK LKLSTTFLST SPNIALLTQN
     LLDALATALS LERVAAENLR AGVQSDFVSS GADQDWEIIA L
//
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Ontology (8)   
   GO (8)   
Chemical substance (4)   
   KEGG COMPOUND (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (33)   
   InterPro (19)   
   Pfam (6)   
   PROSITE (2)   
   Blocks (6)   
Literature (2)   
   PubMed (2)   
All databases (48)   
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