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Database: UniProt
Entry: O54593
LinkDB: O54593
Original site: O54593 
ID   O54593_AMYMD            Unreviewed;      3413 AA.
AC   O54593;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   19-JAN-2010, entry version 65.
DE   SubName: Full=RifE;
DE   SubName: Full=Rifamycin polyketide synthase, type 1;
GN   Name=rifE;
OS   Amycolatopsis mediterranei (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=33910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S699;
RX   MEDLINE=98174059; PubMed=9512878; DOI=10.1016/S1074-5521(98)90141-7;
RA   August P.R., Tang L., Yoon Y.J., Ning S., Muller R., Yu T.W.,
RA   Taylor M., Hoffmann D., Kim C.G., Zhang X., Hutchinson C.R.,
RA   Floss H.G.;
RT   "Biosynthesis of the ansamycin antibiotic rifamycin: deductions from
RT   the molecular analysis of the rif biosynthetic gene cluster of
RT   Amycolatopsis mediterranei S699.";
RL   Chem. Biol. 5:69-79(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S699;
RX   MEDLINE=98165773; PubMed=9497318; DOI=10.1074/jbc.273.11.6030;
RA   Kim C.G., Yu T.W., Fryhle C.B., Handa S., Floss H.G.;
RT   "3-amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the
RT   formation of the precursor of mC7N units in rifamycin and related
RT   antibiotics.";
RL   J. Biol. Chem. 273:6030-6040(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S699;
RX   MEDLINE=21201076; PubMed=11278540; DOI=10.1074/jbc.M009667200;
RA   Yu T.W., Muller R., Muller M., Zhang X., Draeger G., Kim C.G.,
RA   Leistner E., Floss H.G.;
RT   "Mutational analysis and reconstituted expression of the biosynthetic
RT   genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the
RT   starter unit of rifamycin biosynthesis in amycolatopsis Mediterranei
RT   S699.";
RL   J. Biol. Chem. 276:12546-12555(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S699;
RA   Yu T.-W., Pogosova-Agadjanyan E.L., Kuan L.-Y., Bai L., Tin A.M.,
RA   Adman E., Floss H.G.;
RT   "Rifamycin insusceptibility: exploring the rif gene cluster of
RT   Amycolatopsis mediterranei S699.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S699;
RA   Yu T., August P.R., Tang L., Yoon Y.J., Ning S., Mueller R.,
RA   Taylor M., Kim C., Zhang X., Pogosova-Agadjanyan E.L., Tin A.M.,
RA   Hutchinson C.R., Floss H.G.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LBG A3136;
RA   Schupp T., Toupet C., Engel N., Goff S.;
RT   "Cloning and sequence analysis of the putative rifamycin polyketide
RT   synthase gene cluster from Amycolatopsis mediterranei.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF040570; AAC01714.1; -; Genomic_DNA.
DR   EMBL; AJ223012; CAA11039.1; -; Genomic_DNA.
DR   PIR; T17467; T17467.
DR   HSSP; P25715; 1MLA.
DR   SMR; O54593; 30-900, 1592-1684, 2945-3283, 3319-3409.
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: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; IPR002198; DH_sc/Rdtase_SDR.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
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; 2.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 4.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00698; Acyl_transf_1; 2.
DR   Pfam; PF00106; adh_short; 2.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 2.
DR   SMART; SM00822; PKS_KR; 2.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   PROSITE; PS50075; ACP_DOMAIN; 2.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine; Transferase.
FT   CHAIN         1   1701       polyketide synthase module 9.
FT                                /FTId=PRO_5000053972.
FT   CHAIN        31    453       ketoacyl synthase.
FT                                /FTId=PRO_5000053973.
FT   CHAIN       557    875       malonyl acyltransferase.
FT                                /FTId=PRO_5000053974.
FT   CHAIN       887   1087       dehydratase.
FT                                /FTId=PRO_5000053975.
FT   CHAIN      1338   1577       ketoreductase.
FT                                /FTId=PRO_5000053976.
FT   CHAIN      1610   1684       acyl carrier protein.
FT                                /FTId=PRO_5000053977.
FT   CHAIN      1702   3413       polyketide synthase module 10.
FT                                /FTId=PRO_5000053979.
FT   CHAIN      1702   2126       ketoacyl synthase.
FT                                /FTId=PRO_5000053978.
FT   CHAIN      2231   2544       methylmalonyl acyltransferase.
FT                                /FTId=PRO_5000053980.
FT   CHAIN      2554   2754       dehydratase.
FT                                /FTId=PRO_5000053981.
FT   CHAIN      3054   3303       ketoreductase.
FT                                /FTId=PRO_5000053982.
FT   CHAIN      3336   3410       acyl carrier protein.
FT                                /FTId=PRO_5000053983.
SQ   SEQUENCE   3413 AA;  353733 MW;  FFA25AC4A3920AA4 CRC64;
     MATDEKLLKY LKRVTAELHS LRKQGARHAD EPLAVVGMAC RFPGGVSSPE DLWQLVAGGV
     DALSDFPDDR GWELDGLFDP DPDHPGTSYT SQGGFLRGAG LFDAGLFGIS PREALVMDPQ
     QRVLLETSWE ALEDAGVDPL SLKGSDVGVF SGVFTQGYGA GAITPDLEAF AGIGAASSVA
     SGRVSYVFGL EGPAVTIDTA CSSSLVAIHL AAQALRAGEC SMALAGGATV MPTPGTFVAF
     SRQRVLAADG RSKAFSSTAD GTGWAEGAGV LVLERLSVAQ ERGHRILAVL RGSAVNQDGA
     SNGLTAPNGP SQQRVIRKAL AGAGLVASDV DVVEAHGTGT ALGDPIEAQA LLATYGQGRE
     RPLWLGSVKS NFGHTQAAAG VAGVIKMVQA LRHGAMPPTL HVAEPTPEVD WSAGAVELLT
     EPREWPAGDR PRRAGVSAFG ISGTNAHLIL EEAPPADAVA EEPEFKGPVP LVVSAGSPTS
     LAAQAGRLAE VLASGGVSRA RLASGLLSGR ALLGDRAVVV AGTDEDAVAG LRALARGDRA
     PGVLTGSAKH GKVVYVFPGQ GSQRLGMGRE LYDRYPVFAT AFDEACEQLD VCLAGRAGHR
     VRDVVLGEVP AETGLLNQTV FTQAGLFAVE SALFRLAESW GVRPDVVLGH SIGEITAAYA
     AGVFSLPDAA RIVAARGRLM QALAPGGAMV AVAASEAEVA ELLGDGVELA AVNGPSAVVL
     SGDADAVVAA AARMRERGHK TKQLKVSHAF HSARMAPMLA EFAAELAGVT WREPEIPVVS
     NVTGRFAEPG ELTEPGYWAE HVRRPVRFAE GVAAATESGG SLFVELGPGA ALTALVEETA
     EVTCVAALRD DRPEVTALIT AVAELFVRGV AVDWPALLPP VTGFVDLPKY AFDQQHYWLQ
     PAAQATDAAS LGQVAADHPL LGAVVRLPQS DGLVFTSRLS LKSHPWLADH VIGGVVLVAG
     TGLVELAVRA GDEAGCPVLE ELVIEAPLVV PDHGGVRIQV VVGAPGETGS RAVEVYSLRE
     DAGAEVWARH ATGFLAATPS QHKPFDFTAW PPPGVERVDV EDFYDGLVDR GYAYGPSFRG
     LRAVWRRGDE VFAEVALAED DRADAARFGI HPGLLDAALH AGMAGATTTE EPGRPVLPFA
     WNGLVLHAAG ASALRVRLAP SGPDALSVEA ADEAGGLVVT ADSLVSRPVS AEQLGAAANH
     DALFRVEWTE ISSAGDVPAD HVEVLEAVGE DPLELTGRVL EAVQTWLADA ADDARLVVVT
     RGAVHEVTDP AGAAVWGLIR AAQAENPDRI VLLDTDGEVP LGRVLATGEP QTAVRGATLF
     APRLARAEAA EAPAVTGGTV LISGAGSLGA LTARHLVARH GVRRLVLVSR RGPDADGMAE
     LTAELIAQGA EVAVVACDLA DRDQVRVLLA EHRPNAVVHT AGVLDDGVFE SLTRERLAKV
     FAPKVTAANH LDELTRELDL RAFVVFSSAS GVFGSAGQGN YAAANAYLDA VVANRRAAGL
     PGTSLAWGLW EQTDGMTAHL GDADQARASR GGVLAISPAE GMELFDAAPD GLVVPVKLDL
     RKTRAGGTVP HLLRGLVRPG RQQARPASTV DNGLAGRLAG LAPAEQEALL LDVVRTQVAL
     VLGHAGPEAV RADTAFKDTG FDSLTSVELR NRLREASGLK LPATLVFDYP TPVALARYLR
     DELGDTVATT PVATAAAADA GEPIAIVGMA CRLPGGVTDP EGLWRLVRDG LEGLSPFPED
     RGWDLENLFD DDPDRSGTTY TSRGGFLDGA GLFDAGFFGI SPREALAMDP QQRLLLEAAW
     EALEGTGVDP GSLKGADVGV FAGVSNQGYG MGADPAELAG YASTAGASSV VSGRVSYVFG
     FEGPAVTIDT ACSSSLVAMH LAGQALRQGE CSMALAGGVT VMGTPGTFVE FAKQRGLAGD
     GRCKAYAEGA DGTGWAEGVG VVVLERLSVA RERGHRVLAV LRGSAVNSDG ASNGLTAPNG
     PSQQRVIRRA LAGAGLEPSD VDIVEGHGTG TALGDPIEAQ ALLATYGKDR DPETPLWLGS
     VKSNFGHTQS AAGVAGVIKM VQALRHGVMP PTLHVDRPTS QVDWSAGAVE VLTEAREWPR
     NGRPRRAGVS SFGISGTNAH LIIEEAPAEP QLAGPPPDGG VVPLVVSARS PGALAGQARR
     LATFLGDGPL SDVAGALTSR ALFGERAVVV ADSAEEARAG LGALARGEDA PGLVRGRVPA
     SGLPGKLVWV FPGQGTQWVG MGRELLEESP VFAERIAECA AALEPWIGWS LFDVLRGDGD
     LDRVDVLQPA CFAVMVGLAA VWSSAGVVPD AVLGHSQGEI AAACVSGALS LEDAAKVVAL
     RSQAIAAKLS GRGGMASVAL GEADVVSRLA DGVEVAAVNG PASVVIAGDA QALDETLEAL
     SGAGIRARRV AVDYASHTRH VEDIEDTLAE ALAGIDARAP LVPFLSTLTG EWIRDEGVVD
     GGYWYRNLRG RVRFGPAVEA LLAQGHGVFV ELSAHPVLVQ PITELTDETA AVVTGSLRRD
     DGGLRRLLTS MAELFVRGVE VDWTSLVPPA RADLPTYAFD HEHYWLRAAD TASDAVSLGL
     AGADHPLLGA VVQLPQSDGL VFTSRLSLRS HPWLADHAVR DVVIVPGTGL VELAVRAGDE
     AGCPVLDELV IEAPLVVPRR GGVRVQVALG GPADDGSRTV DVFSLREDAD SWLRHATGVL
     VPENRPRGTA AFDFAAWPPP EAKPVDLTGA YDVLADVGYG YGPTFRAVRA VWRRGSGNTT
     ETFAEIALPE DARAEAGRFG IHPALLDAAL HSTMVSAAAD TESYGDEVRL PFAWNGLRLH
     AAGASVLRVR VAKPERDSLS LEAVDESGGL VVTLDSLVGR PVSNDQLTTA AGPAGAGSLY
     RVDWTPLSSV DTSGRVPSWL PVATAEEVAT LADDVLTGAT EAPAVAVMEA VADEGSVLAL
     TVRVLDVVQC WLAGGGLEGT KLAIVTRGAV PAGDGVVHDP AAAAVWGLVR AAQAENPDRI
     VLLDVEPEAD VPPLLGSVLA DGEPQVAVRG TTLSIPRLAR AARPDPAAGF KTRGPVLVTG
     GTGSLGGLVA RHLVERHGVR QLVLASRRGL DAEGAKDLVT DLTALGADVA VAACDVADRD
     QVAALLTEHR PSAVVHTAGV PDAGVIGTVT PDRLAEVFAP KVTAARHLDE LTRDLDLDSF
     VVYSSVSAVF MGAGSGSYAA ANAYLDGLMA HRRAAGLPGQ SLAWGLWDQT TGGMAAGTDE
     AGRARMTRRG GLVAMKPAAG LDLFDAAIGS GEPLLVPAQL DLRGLRAEAA GGTEVPHLLR
     GLVRAGRQQA RAASTVEENW AGRLAGLEPA ERGQVLLELV RAQVAGVLGY RAAHQVDPDQ
     GLFEIGFDSL TAIELRNRLR ARTERKISPG VVFDHPTPAL LAAHLNELLR KKV
//
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Ontology (6)   
   GO (6)   
Chemical substance (1)   
   KEGG COMPOUND (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (32)   
   InterPro (21)   
   Pfam (6)   
   PROSITE (3)   
   Blocks (2)   
Literature (3)   
   PubMed (3)   
All databases (44)   
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