O54593 (O54593_AMYMD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
RifE EMBL AAC01714.1

Submitted name:
Rifamycin polyketide synthase, type 1 EMBL CAA11039.1

Gene names

Name:

rifE EMBL AAC01714.1

Organism

Amycolatopsis mediterranei (Nocardia mediterranei) EMBL AAC01714.1

Taxonomic identifier

33910 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis

Protein attributes

Sequence length	3413 AA.
Sequence status	Complete.
Protein existence	Predicted

Ontologies

Keywords
Ligand	Phosphopantetheine RuleBase RU000721
Molecular function	Transferase RuleBase RU000693
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1701	1701	polyketide synthase module 9 EMBL AAC01714.1		PRO_5000053972
	Chain	31 – 453	423	ketoacyl synthase EMBL AAC01714.1		PRO_5000053973
	Chain	557 – 875	319	malonyl acyltransferase EMBL AAC01714.1		PRO_5000053974
	Chain	887 – 1087	201	dehydratase EMBL AAC01714.1		PRO_5000053975
	Chain	1338 – 1577	240	ketoreductase EMBL AAC01714.1		PRO_5000053976
	Chain	1610 – 1684	75	acyl carrier protein EMBL AAC01714.1		PRO_5000053977
	Chain	1702 – 3413	1712	polyketide synthase module 10 EMBL AAC01714.1		PRO_5000053979
	Chain	1702 – 2126	425	ketoacyl synthase EMBL AAC01714.1		PRO_5000053978
	Chain	2231 – 2544	314	methylmalonyl acyltransferase EMBL AAC01714.1		PRO_5000053980
	Chain	2554 – 2754	201	dehydratase EMBL AAC01714.1		PRO_5000053981
	Chain	3054 – 3303	250	ketoreductase EMBL AAC01714.1		PRO_5000053982
	Chain	3336 – 3410	75	acyl carrier protein EMBL AAC01714.1		PRO_5000053983

Sequences

	Sequence		Length	Mass (Da)
	O54593 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: FFA25AC4A3920AA4	FASTA	3,413	353,733
	10 20 30 40 50 60 MATDEKLLKY LKRVTAELHS LRKQGARHAD EPLAVVGMAC RFPGGVSSPE DLWQLVAGGV 70 80 90 100 110 120 DALSDFPDDR GWELDGLFDP DPDHPGTSYT SQGGFLRGAG LFDAGLFGIS PREALVMDPQ 130 140 150 160 170 180 QRVLLETSWE ALEDAGVDPL SLKGSDVGVF SGVFTQGYGA GAITPDLEAF AGIGAASSVA 190 200 210 220 230 240 SGRVSYVFGL EGPAVTIDTA CSSSLVAIHL AAQALRAGEC SMALAGGATV MPTPGTFVAF 250 260 270 280 290 300 SRQRVLAADG RSKAFSSTAD GTGWAEGAGV LVLERLSVAQ ERGHRILAVL RGSAVNQDGA 310 320 330 340 350 360 SNGLTAPNGP SQQRVIRKAL AGAGLVASDV DVVEAHGTGT ALGDPIEAQA LLATYGQGRE 370 380 390 400 410 420 RPLWLGSVKS NFGHTQAAAG VAGVIKMVQA LRHGAMPPTL HVAEPTPEVD WSAGAVELLT 430 440 450 460 470 480 EPREWPAGDR PRRAGVSAFG ISGTNAHLIL EEAPPADAVA EEPEFKGPVP LVVSAGSPTS 490 500 510 520 530 540 LAAQAGRLAE VLASGGVSRA RLASGLLSGR ALLGDRAVVV AGTDEDAVAG LRALARGDRA 550 560 570 580 590 600 PGVLTGSAKH GKVVYVFPGQ GSQRLGMGRE LYDRYPVFAT AFDEACEQLD VCLAGRAGHR 610 620 630 640 650 660 VRDVVLGEVP AETGLLNQTV FTQAGLFAVE SALFRLAESW GVRPDVVLGH SIGEITAAYA 670 680 690 700 710 720 AGVFSLPDAA RIVAARGRLM QALAPGGAMV AVAASEAEVA ELLGDGVELA AVNGPSAVVL 730 740 750 760 770 780 SGDADAVVAA AARMRERGHK TKQLKVSHAF HSARMAPMLA EFAAELAGVT WREPEIPVVS 790 800 810 820 830 840 NVTGRFAEPG ELTEPGYWAE HVRRPVRFAE GVAAATESGG SLFVELGPGA ALTALVEETA 850 860 870 880 890 900 EVTCVAALRD DRPEVTALIT AVAELFVRGV AVDWPALLPP VTGFVDLPKY AFDQQHYWLQ 910 920 930 940 950 960 PAAQATDAAS LGQVAADHPL LGAVVRLPQS DGLVFTSRLS LKSHPWLADH VIGGVVLVAG 970 980 990 1000 1010 1020 TGLVELAVRA GDEAGCPVLE ELVIEAPLVV PDHGGVRIQV VVGAPGETGS RAVEVYSLRE 1030 1040 1050 1060 1070 1080 DAGAEVWARH ATGFLAATPS QHKPFDFTAW PPPGVERVDV EDFYDGLVDR GYAYGPSFRG 1090 1100 1110 1120 1130 1140 LRAVWRRGDE VFAEVALAED DRADAARFGI HPGLLDAALH AGMAGATTTE EPGRPVLPFA 1150 1160 1170 1180 1190 1200 WNGLVLHAAG ASALRVRLAP SGPDALSVEA ADEAGGLVVT ADSLVSRPVS AEQLGAAANH 1210 1220 1230 1240 1250 1260 DALFRVEWTE ISSAGDVPAD HVEVLEAVGE DPLELTGRVL EAVQTWLADA ADDARLVVVT 1270 1280 1290 1300 1310 1320 RGAVHEVTDP AGAAVWGLIR AAQAENPDRI VLLDTDGEVP LGRVLATGEP QTAVRGATLF 1330 1340 1350 1360 1370 1380 APRLARAEAA EAPAVTGGTV LISGAGSLGA LTARHLVARH GVRRLVLVSR RGPDADGMAE 1390 1400 1410 1420 1430 1440 LTAELIAQGA EVAVVACDLA DRDQVRVLLA EHRPNAVVHT AGVLDDGVFE SLTRERLAKV 1450 1460 1470 1480 1490 1500 FAPKVTAANH LDELTRELDL RAFVVFSSAS GVFGSAGQGN YAAANAYLDA VVANRRAAGL 1510 1520 1530 1540 1550 1560 PGTSLAWGLW EQTDGMTAHL GDADQARASR GGVLAISPAE GMELFDAAPD GLVVPVKLDL 1570 1580 1590 1600 1610 1620 RKTRAGGTVP HLLRGLVRPG RQQARPASTV DNGLAGRLAG LAPAEQEALL LDVVRTQVAL 1630 1640 1650 1660 1670 1680 VLGHAGPEAV RADTAFKDTG FDSLTSVELR NRLREASGLK LPATLVFDYP TPVALARYLR 1690 1700 1710 1720 1730 1740 DELGDTVATT PVATAAAADA GEPIAIVGMA CRLPGGVTDP EGLWRLVRDG LEGLSPFPED 1750 1760 1770 1780 1790 1800 RGWDLENLFD DDPDRSGTTY TSRGGFLDGA GLFDAGFFGI SPREALAMDP QQRLLLEAAW 1810 1820 1830 1840 1850 1860 EALEGTGVDP GSLKGADVGV FAGVSNQGYG MGADPAELAG YASTAGASSV VSGRVSYVFG 1870 1880 1890 1900 1910 1920 FEGPAVTIDT ACSSSLVAMH LAGQALRQGE CSMALAGGVT VMGTPGTFVE FAKQRGLAGD 1930 1940 1950 1960 1970 1980 GRCKAYAEGA DGTGWAEGVG VVVLERLSVA RERGHRVLAV LRGSAVNSDG ASNGLTAPNG 1990 2000 2010 2020 2030 2040 PSQQRVIRRA LAGAGLEPSD VDIVEGHGTG TALGDPIEAQ ALLATYGKDR DPETPLWLGS 2050 2060 2070 2080 2090 2100 VKSNFGHTQS AAGVAGVIKM VQALRHGVMP PTLHVDRPTS QVDWSAGAVE VLTEAREWPR 2110 2120 2130 2140 2150 2160 NGRPRRAGVS SFGISGTNAH LIIEEAPAEP QLAGPPPDGG VVPLVVSARS PGALAGQARR 2170 2180 2190 2200 2210 2220 LATFLGDGPL SDVAGALTSR ALFGERAVVV ADSAEEARAG LGALARGEDA PGLVRGRVPA 2230 2240 2250 2260 2270 2280 SGLPGKLVWV FPGQGTQWVG MGRELLEESP VFAERIAECA AALEPWIGWS LFDVLRGDGD 2290 2300 2310 2320 2330 2340 LDRVDVLQPA CFAVMVGLAA VWSSAGVVPD AVLGHSQGEI AAACVSGALS LEDAAKVVAL 2350 2360 2370 2380 2390 2400 RSQAIAAKLS GRGGMASVAL GEADVVSRLA DGVEVAAVNG PASVVIAGDA QALDETLEAL 2410 2420 2430 2440 2450 2460 SGAGIRARRV AVDYASHTRH VEDIEDTLAE ALAGIDARAP LVPFLSTLTG EWIRDEGVVD 2470 2480 2490 2500 2510 2520 GGYWYRNLRG RVRFGPAVEA LLAQGHGVFV ELSAHPVLVQ PITELTDETA AVVTGSLRRD 2530 2540 2550 2560 2570 2580 DGGLRRLLTS MAELFVRGVE VDWTSLVPPA RADLPTYAFD HEHYWLRAAD TASDAVSLGL 2590 2600 2610 2620 2630 2640 AGADHPLLGA VVQLPQSDGL VFTSRLSLRS HPWLADHAVR DVVIVPGTGL VELAVRAGDE 2650 2660 2670 2680 2690 2700 AGCPVLDELV IEAPLVVPRR GGVRVQVALG GPADDGSRTV DVFSLREDAD SWLRHATGVL 2710 2720 2730 2740 2750 2760 VPENRPRGTA AFDFAAWPPP EAKPVDLTGA YDVLADVGYG YGPTFRAVRA VWRRGSGNTT 2770 2780 2790 2800 2810 2820 ETFAEIALPE DARAEAGRFG IHPALLDAAL HSTMVSAAAD TESYGDEVRL PFAWNGLRLH 2830 2840 2850 2860 2870 2880 AAGASVLRVR VAKPERDSLS LEAVDESGGL VVTLDSLVGR PVSNDQLTTA AGPAGAGSLY 2890 2900 2910 2920 2930 2940 RVDWTPLSSV DTSGRVPSWL PVATAEEVAT LADDVLTGAT EAPAVAVMEA VADEGSVLAL 2950 2960 2970 2980 2990 3000 TVRVLDVVQC WLAGGGLEGT KLAIVTRGAV PAGDGVVHDP AAAAVWGLVR AAQAENPDRI 3010 3020 3030 3040 3050 3060 VLLDVEPEAD VPPLLGSVLA DGEPQVAVRG TTLSIPRLAR AARPDPAAGF KTRGPVLVTG 3070 3080 3090 3100 3110 3120 GTGSLGGLVA RHLVERHGVR QLVLASRRGL DAEGAKDLVT DLTALGADVA VAACDVADRD 3130 3140 3150 3160 3170 3180 QVAALLTEHR PSAVVHTAGV PDAGVIGTVT PDRLAEVFAP KVTAARHLDE LTRDLDLDSF 3190 3200 3210 3220 3230 3240 VVYSSVSAVF MGAGSGSYAA ANAYLDGLMA HRRAAGLPGQ SLAWGLWDQT TGGMAAGTDE 3250 3260 3270 3280 3290 3300 AGRARMTRRG GLVAMKPAAG LDLFDAAIGS GEPLLVPAQL DLRGLRAEAA GGTEVPHLLR 3310 3320 3330 3340 3350 3360 GLVRAGRQQA RAASTVEENW AGRLAGLEPA ERGQVLLELV RAQVAGVLGY RAAHQVDPDQ 3370 3380 3390 3400 3410 GLFEIGFDSL TAIELRNRLR ARTERKISPG VVFDHPTPAL LAAHLNELLR KKV

References

[1]	"Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699." August P.R., Tang L., Yoon Y.J., Ning S., Muller R., Yu T.W., Taylor M., Hoffmann D., Kim C.G., Zhang X., Hutchinson C.R., Floss H.G. Chem. Biol. 5:69-79(1998) [PubMed: 9512878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01714.1.
[2]	"Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in amycolatopsis Mediterranei S699." Yu T.W., Muller R., Muller M., Zhang X., Draeger G., Kim C.G., Leistner E., Floss H.G. J. Biol. Chem. 276:12546-12555(2001) [PubMed: 11278540] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01714.1.
[3]	"3-amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics." Kim C.G., Yu T.W., Fryhle C.B., Handa S., Floss H.G. J. Biol. Chem. 273:6030-6040(1998) [PubMed: 9497318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01714.1.
[4]	"Rifamycin insusceptibility: exploring the rif gene cluster of Amycolatopsis mediterranei S699." Yu T.-W., Pogosova-Agadjanyan E.L., Kuan L.-Y., Bai L., Tin A.M., Adman E., Floss H.G. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01714.1.
[5]	"Cloning and sequence analysis of the putative rifamycin polyketide synthase gene cluster from Amycolatopsis mediterranei." Schupp T., Toupet C., Engel N., Goff S. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: LBG A3136 EMBL CAA11039.1.
[6]	Yu T., August P.R., Tang L., Yoon Y.J., Ning S., Mueller R., Taylor M., Kim C., Zhang X., Pogosova-Agadjanyan E.L., Tin A.M., Hutchinson C.R., Floss H.G. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01714.1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF040570 Genomic DNA. Translation: AAC01714.1. AJ223012 Genomic DNA. Translation: CAA11039.1.
PIR	T17467.
3D structure databases
HSSP	HSSP built from PDB template 1MLA based on UniProtKB P25715.
ProteinModelPortal	O54593.
SMR	O54593. Positions 1592-1684.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001227. Ac_transferase_dom. IPR009081. Acyl_carrier_prot-like. IPR014043. Acyl_transferase. IPR016035. Acyl_Trfase/lysoPLipase. IPR000794. Beta-ketoacyl_synthase. IPR002198. DH_sc/Rdtase_SDR. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016036. Malonyl_transacylase_ACP-bd. IPR016040. NAD(P)-bd_dom. IPR006163. Phsphopanteth-bd. IPR020842. PKS/FAS_KR. IPR020801. PKS_acyl_transferase. IPR020841. PKS_Beta-ketoAc_synthase_dom. IPR020807. PKS_dehydratase. IPR020806. PKS_PP-bd. IPR015083. Polyketide_synth_docking. IPR006162. PPantetheine_attach_site. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.366.10. Ac_transferase_reg. 4 hits. G3DSA:1.10.1200.10. ACP_like. 2 hits. G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
PANTHER	PTHR11712. Ketoacyl_synth. 1 hit.
Pfam	PF00698. Acyl_transf_1. 2 hits. PF00106. adh_short. 2 hits. PF08990. Docking. 1 hit. PF00109. ketoacyl-synt. 2 hits. PF02801. Ketoacyl-synt_C. 2 hits. PF00550. PP-binding. 2 hits. [Graphical view]
SMART	SM00827. PKS_AT. 2 hits. SM00826. PKS_DH. 2 hits. SM00822. PKS_KR. 2 hits. SM00825. PKS_KS. 2 hits. SM00823. PKS_PP. 2 hits. [Graphical view]
SUPFAM	SSF47336. ACP_like. 2 hits. SSF52151. Acyl_Trfase/lysoPlipase. 2 hits. SSF55048. Malonyl_transacylase_ACP-bd. 2 hits. SSF53901. Thiolase-like. 2 hits.
PROSITE	PS50075. ACP_DOMAIN. 2 hits. PS00606. B_KETOACYL_SYNTHASE. 2 hits. PS00012. PHOSPHOPANTETHEINE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

O54593_AMYMD

Accession

Primary (citable) accession number: O54593

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 1998
Last sequence update:	June 1, 1998
Last modified:	December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)