ID O54591_AMYMD Unreviewed; 1728 AA.
AC O54591;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 19-JAN-2010, entry version 62.
DE SubName: Full=RifD;
DE SubName: Full=Rifamycin polyketide synthase, type 1;
GN Name=rifD;
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; AAC01713.1; -; Genomic_DNA.
DR EMBL; AJ223012; CAA11038.1; -; Genomic_DNA.
DR PIR; T17466; T17466.
DR SMR; O54591; 4-905, 1273-1649.
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; 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; PF08990; Docking; 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.
FT CHAIN 1 1728 polyketide synthase module 8.
FT /FTId=PRO_5000053966.
FT CHAIN 34 460 ketoacyl synthase.
FT /FTId=PRO_5000053967.
FT CHAIN 566 882 methylmalonyl acyltransferase.
FT /FTId=PRO_5000053968.
FT CHAIN 892 1058 dehydratase.
FT /FTId=PRO_5000053969.
FT CHAIN 1300 1542 ketoreductase.
FT /FTId=PRO_5000053970.
FT CHAIN 1575 1649 acyl carrier protein.
FT /FTId=PRO_5000053971.
SQ SEQUENCE 1728 AA; 180056 MW; C8046279CA1F6657 CRC64;
MADEGQLRDY LKRAIADARD ARTRLREVEE QAREPIAIVA MACRYPGGVS SPEDLWRLVA
EGTDAVSAFP GDRGWDVDGL VDPDPDRPGT TYTDQGGFLH EAGLFDAGFF GISPREAVAM
DPQQRLLLET SWEAIERTGT DPLSLKGSDI GVFTGVASMG YGAGGGVVAP ELEGFVGTGA
APCIASGRVS YVLGFEGPAV TVDTGCSSSL VAMHLAAQAL RRGECSMALA GGAMVMAQPG
SFVSFSRQRG LALDGRCKAF SDSADGMGLA EGVGVIALER LSVARERGHR VLAVLRGIAV
NQDGASNGLT APNGPSQQRV IRAALAEAGL SPSDVDAVEG HGTGTTLGDP IEAQALLATY
GKGRDPEKPL WLGSVKSNLG HTQAAAGVAS VIKMVQALRH GVLPPTLHVD RPSTEVDWSA
GAVSLLTEAR EWPREGRPRR AGVSSFGISG TNAHLILEEA PEEEPPVAEA PSAGVVPVVV
SARGALAGQA GRLAAFLEAS DEPLVTVAGA LICGRSRFGD RAVVVAGTRA EATAGLAALA
RGESAADVVT GTVAASGVPG KLVWVFPGQG SQWVGMGREL LEASPVFAAR IAECAAALEP
WIDWSLLDVL RGEGDLDRVD VVQPASFAVM VGLAAVWSSV GVVPDAVLGH SQGEIAAACV
SGALSLQDAA KVVALRSQAI AAKLAGRGGM ASVALSEEDA VARLRHWADR VEVAAVNSPS
SVVIAGDAEA LDQALEALTG QDIRVRRVAV DYASHTRHVE DIQEPLAEAL AGIEAHAPTL
PFFSTLTGDW IREAGVVDGG YWYRNLRNQV GFGPAVAELL GLGHRVFVEV SAHPVLVQAI
SAIADDTDAV VTGSLRREEG GLRRLLTSMA ELFVRGVDVD WATMVPPARV DLPTYAFDHQ
HYWLRYVETA TDAAGPVVRL PQTGGLVFTT EWSLKSQPWL AEHTLEDLVV VPGAALVELA
VRAGDEAGTP VLDELVIETP LVVPERGAIR VQVTVSGPDD GTRTLEVHSQ PEDATDEWTR
HATGTLSATP DESSGFDFTA WPPPGARQLD GVPAIWRAGD EIFAEVSLPD DADAEAFGIH
PALLDAALHP ALPGDDGLTQ PMEWRGLTLH AAGASTLRVR LVPGGFLEAA DGAGSLVVTA
KEVALRPVTI ARSRTTTRDS LFQLNWIELP ESGVVAAADD TEVLEVPAGD SPLAATSRVL
ERLQTWLTEP EAEQLVVVTR GAVPAGDTPV TDPAAAAVWG LVRSAQAENP DRIVLLDTDG
EVPLGAVLAG GEPQVAVRGT ALYVPRLARA DAAPVSGLHG TVLVSGAGVL GEIVARHLVT
RHGVRKLVLA SRRGLDADGA KDLVTDLTGE GADVSVVACD LADRNQVAAL LADHRPASVI
HTAGVLDDGV IGTLTPERLA KVFAPKVDAV RHLDELTRDL DLDAFVVFSS GSGVFGSPGQ
GNYAAANAFL DAAMASRRAA GLPGLSLAWG LWEQATGMTA HLGGTDQARM SRGGVRPITA
EEGMALFDTA LGAQPALLVP VKLDLREVRA GGAVPHLLRG LVRAGRRQAQ AASTVDNQLL
GRLAGLGAPE QEALLVDLVR GQVAAVLGHA GPDAVRADTA FKDAGFDSLT SVDLRNRLRE
STGLKLPATL AFDYPTPLVL ARHLRDELGA GDDALSVVHA RLEDVEALLG GLRLDESTKT
GLTLRLQGLV ARCNGVNDQT GGETLADRLE AASADEVLDF IDEELGLT
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