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Database: UniProt
Entry: O52790
LinkDB: O52790
Original site: O52790 
ID   O52790_AMYMD            Unreviewed;      1763 AA.
AC   O52790; O52546;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   19-JAN-2010, entry version 67.
DE   SubName: Full=RifC;
DE   SubName: Full=Rifamycin polyketide synthase, type 1;
GN   Name=rifC;
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=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.
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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.
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DR   EMBL; AF040570; AAC01712.2; -; Genomic_DNA.
DR   EMBL; AJ223012; CAA11037.1; -; Genomic_DNA.
DR   PIR; T17465; T17465.
DR   HSSP; P72391; 1NM2.
DR   SMR; O52790; 7-894, 1228-1564, 1322-1691.
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; 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; PF00106; adh_short; 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; 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   1763 AA;  182823 MW;  DCD7FD776F006692 CRC64;
     MVSASYEKVV EALRKSLEEV GTLKKRNRQL ADAAGEPIAI VGMACRLPGG VTGPGDLWRL
     VAEGGDAVSG FPTDRCWDLD TLFDPDPDHA GTSYTDQGGF LHDAALFDPG FFGISPREAL
     AMDPQQRLLL EASWEALEGV GLDPASLQGT DVGVFTGAGG SGYGGGLTGP EMQSFAGTGL
     ASSVASGRVS YVFGFEGPAV TIDTACSSSL VAMHLAAQAL RQGDCSMALA GGAMVMSGPD
     SFVVFSRQRG LATDGRCKAF ASGADGMVLA EGISVVVLER LSVARERGHR VLAVLRGSAV
     NQDGASNGLT APNGPSQQRV IRAALANAGI GPSDVDLVEA HGTGTSLGDP IEAQALLATY
     GQDRETPLWL GSLKSNIGHT QAAAGVASVI KVVQALRHGV MPPTLHVDEP SSQVDWSEGA
     VELLTGSRDW PRGDRPRRAG VSSFGVSGTN VHLIIEEAPE EPAAAVPTSA DVVPLVVSAR
     STGSLAGQAD RLTEVDVPLG HLAGALVAGR AVLEERAVVV AGSAEEARAG LGALARGEAA
     PGVVTGTAGK PGKVVWVFPG QGTQWVGMGR ELLDASPVFA ERIKECAAAL DQWTDWSLLD
     VLRGDGDLDS VEVLQPACFA VMVGLAAVWE SAGVRPDAVV GHSQGEIAAA CVSGALTLDD
     AAKVVALRSQ AIAARLSGRG GMASVALSED EANARLGLWD GRIEVAAVNG PASVVIAGDA
     QALDEALEVL AGDGVRVRQV AVDYASHTRH VEDIRDTLAE TLAGITAQAP DVPFRSTVTG
     GWVRDADVLD GGYWYRNLRN QVRFGPAVAE LLEQGHGVFV EVSAHPVLVQ PISELTDAVV
     TGTLRRDDGG LRRLLTSMAE LFVRGVRVDW ATLVPPARVD LPTYAFDHQH FWLRPAAQAD
     AVSLGQAAAE HPLLGAVVRL PQSDGLVFTS RLSLRTHPWL ADHTIGGVVL FPGTGLVELA
     VRAGDEAGCP VLDELVTEAP LVVPGQGGVN VQVTVSGPDQ NGLRTVDIHS QRDDVWTRHA
     TGTVSATPAS SPGFDFTAWP PPDGQRVEIG DFYADLAERG YAYGPLFQGV RAVWQRGEDV
     FAEVALPEDR REDAARFGLH PALLDAALQT GTIAAAASGQ PGKSVMPFSW NRLALHAVGA
     AGLRVRVAPG GPDALTVEAA DETGAPVLTM DSLILREVAL DQLDTARAGS LYRVDWTPLP
     TVDSAVPAGR AEVLEAFGEE PLDLTGRVLA ALQAWLSDAA EEARLVVVTR GAVPAGDGVV
     SDPAGAAVWG LVRAAQAENP DRFVLLDTDG EVPLEAVLAT GEPQLALRGT TFSVPRLARV
     TEPAEAPLTF RPDGTVLVSG AGTLGALAAR DLVTRHGVRR LVLASRRGRA AEGIDDLVAE
     LTGHGAEVTV AACDVSDRDQ VAALLKEHAL TAVVHTAGVF DAGVTGALTR ERLAKVFAPK
     VDAANHLDEL TRDLDLDAFI VYSSASSIFM GAGSGGYAAA NAYLDGLMAA RRAAGLPGLS
     LAWGPWEQLT GMADTIDDLT LARMSRREGR GGVRALGSAD GMELFDAALA AGQALLVPIE
     LDLREVRADA AGGGTVPHLL RGLVRAGRQA ARTAATEDGG LERRLAGLTV AEQEALLLDL
     VRGQVAVVLG HADSSGVRAD AAFKDAGFDS LTSVELRNRL RETTGLKLPA TLVFDHPNPL
     ALARHLRAEL AVDEASPADA VLAGLAGLEA AIAAAGAPDG DRITARLREL LKAAEAAEAR
     PGTSGDLDTA SDEELFALVD GLD
//
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Ontology (6)   
   GO (6)   
Chemical substance (1)   
   KEGG COMPOUND (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (32)   
   InterPro (20)   
   Pfam (5)   
   PROSITE (3)   
   Blocks (4)   
Literature (3)   
   PubMed (3)   
All databases (44)   
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