O54591 (O54591_AMYMD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
RifD EMBL AAC01713.1

Submitted name:
Rifamycin polyketide synthase, type 1 EMBL CAA11038.1

Gene names

Name:

rifD EMBL AAC01713.1

Organism

Amycolatopsis mediterranei (Nocardia mediterranei) EMBL AAC01713.1

Taxonomic identifier

33910 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1728 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 – 1728	1728	polyketide synthase module 8 EMBL AAC01713.1		PRO_5000053966
	Chain	34 – 460	427	ketoacyl synthase EMBL AAC01713.1		PRO_5000053967
	Chain	566 – 882	317	methylmalonyl acyltransferase EMBL AAC01713.1		PRO_5000053968
	Chain	892 – 1058	167	dehydratase EMBL AAC01713.1		PRO_5000053969
	Chain	1300 – 1542	243	ketoreductase EMBL AAC01713.1		PRO_5000053970
	Chain	1575 – 1649	75	acyl carrier protein EMBL AAC01713.1		PRO_5000053971

Sequences

	Sequence		Length	Mass (Da)
	O54591 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: C8046279CA1F6657	FASTA	1,728	180,056
	10 20 30 40 50 60 MADEGQLRDY LKRAIADARD ARTRLREVEE QAREPIAIVA MACRYPGGVS SPEDLWRLVA 70 80 90 100 110 120 EGTDAVSAFP GDRGWDVDGL VDPDPDRPGT TYTDQGGFLH EAGLFDAGFF GISPREAVAM 130 140 150 160 170 180 DPQQRLLLET SWEAIERTGT DPLSLKGSDI GVFTGVASMG YGAGGGVVAP ELEGFVGTGA 190 200 210 220 230 240 APCIASGRVS YVLGFEGPAV TVDTGCSSSL VAMHLAAQAL RRGECSMALA GGAMVMAQPG 250 260 270 280 290 300 SFVSFSRQRG LALDGRCKAF SDSADGMGLA EGVGVIALER LSVARERGHR VLAVLRGIAV 310 320 330 340 350 360 NQDGASNGLT APNGPSQQRV IRAALAEAGL SPSDVDAVEG HGTGTTLGDP IEAQALLATY 370 380 390 400 410 420 GKGRDPEKPL WLGSVKSNLG HTQAAAGVAS VIKMVQALRH GVLPPTLHVD RPSTEVDWSA 430 440 450 460 470 480 GAVSLLTEAR EWPREGRPRR AGVSSFGISG TNAHLILEEA PEEEPPVAEA PSAGVVPVVV 490 500 510 520 530 540 SARGALAGQA GRLAAFLEAS DEPLVTVAGA LICGRSRFGD RAVVVAGTRA EATAGLAALA 550 560 570 580 590 600 RGESAADVVT GTVAASGVPG KLVWVFPGQG SQWVGMGREL LEASPVFAAR IAECAAALEP 610 620 630 640 650 660 WIDWSLLDVL RGEGDLDRVD VVQPASFAVM VGLAAVWSSV GVVPDAVLGH SQGEIAAACV 670 680 690 700 710 720 SGALSLQDAA KVVALRSQAI AAKLAGRGGM ASVALSEEDA VARLRHWADR VEVAAVNSPS 730 740 750 760 770 780 SVVIAGDAEA LDQALEALTG QDIRVRRVAV DYASHTRHVE DIQEPLAEAL AGIEAHAPTL 790 800 810 820 830 840 PFFSTLTGDW IREAGVVDGG YWYRNLRNQV GFGPAVAELL GLGHRVFVEV SAHPVLVQAI 850 860 870 880 890 900 SAIADDTDAV VTGSLRREEG GLRRLLTSMA ELFVRGVDVD WATMVPPARV DLPTYAFDHQ 910 920 930 940 950 960 HYWLRYVETA TDAAGPVVRL PQTGGLVFTT EWSLKSQPWL AEHTLEDLVV VPGAALVELA 970 980 990 1000 1010 1020 VRAGDEAGTP VLDELVIETP LVVPERGAIR VQVTVSGPDD GTRTLEVHSQ PEDATDEWTR 1030 1040 1050 1060 1070 1080 HATGTLSATP DESSGFDFTA WPPPGARQLD GVPAIWRAGD EIFAEVSLPD DADAEAFGIH 1090 1100 1110 1120 1130 1140 PALLDAALHP ALPGDDGLTQ PMEWRGLTLH AAGASTLRVR LVPGGFLEAA DGAGSLVVTA 1150 1160 1170 1180 1190 1200 KEVALRPVTI ARSRTTTRDS LFQLNWIELP ESGVVAAADD TEVLEVPAGD SPLAATSRVL 1210 1220 1230 1240 1250 1260 ERLQTWLTEP EAEQLVVVTR GAVPAGDTPV TDPAAAAVWG LVRSAQAENP DRIVLLDTDG 1270 1280 1290 1300 1310 1320 EVPLGAVLAG GEPQVAVRGT ALYVPRLARA DAAPVSGLHG TVLVSGAGVL GEIVARHLVT 1330 1340 1350 1360 1370 1380 RHGVRKLVLA SRRGLDADGA KDLVTDLTGE GADVSVVACD LADRNQVAAL LADHRPASVI 1390 1400 1410 1420 1430 1440 HTAGVLDDGV IGTLTPERLA KVFAPKVDAV RHLDELTRDL DLDAFVVFSS GSGVFGSPGQ 1450 1460 1470 1480 1490 1500 GNYAAANAFL DAAMASRRAA GLPGLSLAWG LWEQATGMTA HLGGTDQARM SRGGVRPITA 1510 1520 1530 1540 1550 1560 EEGMALFDTA LGAQPALLVP VKLDLREVRA GGAVPHLLRG LVRAGRRQAQ AASTVDNQLL 1570 1580 1590 1600 1610 1620 GRLAGLGAPE QEALLVDLVR GQVAAVLGHA GPDAVRADTA FKDAGFDSLT SVDLRNRLRE 1630 1640 1650 1660 1670 1680 STGLKLPATL AFDYPTPLVL ARHLRDELGA GDDALSVVHA RLEDVEALLG GLRLDESTKT 1690 1700 1710 1720 GLTLRLQGLV ARCNGVNDQT GGETLADRLE AASADEVLDF IDEELGLT

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 AAC01713.1.
[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 AAC01713.1.
[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 AAC01713.1.
[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 AAC01713.1.
[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 CAA11038.1.
[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 AAC01713.1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF040570 Genomic DNA. Translation: AAC01713.1. AJ223012 Genomic DNA. Translation: CAA11038.1.
PIR	T17466.
3D structure databases
ProteinModelPortal	O54591.
SMR	O54591. Positions 4-905, 1557-1649.
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. 2 hits. G3DSA:1.10.1200.10. ACP_like. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PANTHER	PTHR11712. Ketoacyl_synth. 1 hit.
Pfam	PF00698. Acyl_transf_1. 1 hit. PF00106. adh_short. 1 hit. PF08990. Docking. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF00550. PP-binding. 1 hit. [Graphical view]
SMART	SM00827. PKS_AT. 1 hit. SM00826. PKS_DH. 1 hit. SM00822. PKS_KR. 1 hit. SM00825. PKS_KS. 1 hit. SM00823. PKS_PP. 1 hit. [Graphical view]
SUPFAM	SSF47336. ACP_like. 1 hit. SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF55048. Malonyl_transacylase_ACP-bd. 1 hit. SSF101173. Polyketide_synth_docking. 1 hit. SSF53901. Thiolase-like. 1 hit.
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

O54591_AMYMD

Accession

Primary (citable) accession number: O54591

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 1998
Last sequence update:	June 1, 1998
Last modified:	December 14, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)