O52790 (O52790_AMYMD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
RifC EMBL AAC01712.2

Submitted name:
Rifamycin polyketide synthase, type 1 EMBL CAA11037.1

Gene names

Name:

rifC EMBL AAC01712.2

Organism

Amycolatopsis mediterranei (Nocardia mediterranei) EMBL CAA11037.1

Taxonomic identifier

33910 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1763 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...

Sequences

	Sequence		Length	Mass (Da)
	O52790 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: DCD7FD776F006692	FASTA	1,763	182,823
	10 20 30 40 50 60 MVSASYEKVV EALRKSLEEV GTLKKRNRQL ADAAGEPIAI VGMACRLPGG VTGPGDLWRL 70 80 90 100 110 120 VAEGGDAVSG FPTDRCWDLD TLFDPDPDHA GTSYTDQGGF LHDAALFDPG FFGISPREAL 130 140 150 160 170 180 AMDPQQRLLL EASWEALEGV GLDPASLQGT DVGVFTGAGG SGYGGGLTGP EMQSFAGTGL 190 200 210 220 230 240 ASSVASGRVS YVFGFEGPAV TIDTACSSSL VAMHLAAQAL RQGDCSMALA GGAMVMSGPD 250 260 270 280 290 300 SFVVFSRQRG LATDGRCKAF ASGADGMVLA EGISVVVLER LSVARERGHR VLAVLRGSAV 310 320 330 340 350 360 NQDGASNGLT APNGPSQQRV IRAALANAGI GPSDVDLVEA HGTGTSLGDP IEAQALLATY 370 380 390 400 410 420 GQDRETPLWL GSLKSNIGHT QAAAGVASVI KVVQALRHGV MPPTLHVDEP SSQVDWSEGA 430 440 450 460 470 480 VELLTGSRDW PRGDRPRRAG VSSFGVSGTN VHLIIEEAPE EPAAAVPTSA DVVPLVVSAR 490 500 510 520 530 540 STGSLAGQAD RLTEVDVPLG HLAGALVAGR AVLEERAVVV AGSAEEARAG LGALARGEAA 550 560 570 580 590 600 PGVVTGTAGK PGKVVWVFPG QGTQWVGMGR ELLDASPVFA ERIKECAAAL DQWTDWSLLD 610 620 630 640 650 660 VLRGDGDLDS VEVLQPACFA VMVGLAAVWE SAGVRPDAVV GHSQGEIAAA CVSGALTLDD 670 680 690 700 710 720 AAKVVALRSQ AIAARLSGRG GMASVALSED EANARLGLWD GRIEVAAVNG PASVVIAGDA 730 740 750 760 770 780 QALDEALEVL AGDGVRVRQV AVDYASHTRH VEDIRDTLAE TLAGITAQAP DVPFRSTVTG 790 800 810 820 830 840 GWVRDADVLD GGYWYRNLRN QVRFGPAVAE LLEQGHGVFV EVSAHPVLVQ PISELTDAVV 850 860 870 880 890 900 TGTLRRDDGG LRRLLTSMAE LFVRGVRVDW ATLVPPARVD LPTYAFDHQH FWLRPAAQAD 910 920 930 940 950 960 AVSLGQAAAE HPLLGAVVRL PQSDGLVFTS RLSLRTHPWL ADHTIGGVVL FPGTGLVELA 970 980 990 1000 1010 1020 VRAGDEAGCP VLDELVTEAP LVVPGQGGVN VQVTVSGPDQ NGLRTVDIHS QRDDVWTRHA 1030 1040 1050 1060 1070 1080 TGTVSATPAS SPGFDFTAWP PPDGQRVEIG DFYADLAERG YAYGPLFQGV RAVWQRGEDV 1090 1100 1110 1120 1130 1140 FAEVALPEDR REDAARFGLH PALLDAALQT GTIAAAASGQ PGKSVMPFSW NRLALHAVGA 1150 1160 1170 1180 1190 1200 AGLRVRVAPG GPDALTVEAA DETGAPVLTM DSLILREVAL DQLDTARAGS LYRVDWTPLP 1210 1220 1230 1240 1250 1260 TVDSAVPAGR AEVLEAFGEE PLDLTGRVLA ALQAWLSDAA EEARLVVVTR GAVPAGDGVV 1270 1280 1290 1300 1310 1320 SDPAGAAVWG LVRAAQAENP DRFVLLDTDG EVPLEAVLAT GEPQLALRGT TFSVPRLARV 1330 1340 1350 1360 1370 1380 TEPAEAPLTF RPDGTVLVSG AGTLGALAAR DLVTRHGVRR LVLASRRGRA AEGIDDLVAE 1390 1400 1410 1420 1430 1440 LTGHGAEVTV AACDVSDRDQ VAALLKEHAL TAVVHTAGVF DAGVTGALTR ERLAKVFAPK 1450 1460 1470 1480 1490 1500 VDAANHLDEL TRDLDLDAFI VYSSASSIFM GAGSGGYAAA NAYLDGLMAA RRAAGLPGLS 1510 1520 1530 1540 1550 1560 LAWGPWEQLT GMADTIDDLT LARMSRREGR GGVRALGSAD GMELFDAALA AGQALLVPIE 1570 1580 1590 1600 1610 1620 LDLREVRADA AGGGTVPHLL RGLVRAGRQA ARTAATEDGG LERRLAGLTV AEQEALLLDL 1630 1640 1650 1660 1670 1680 VRGQVAVVLG HADSSGVRAD AAFKDAGFDS LTSVELRNRL RETTGLKLPA TLVFDHPNPL 1690 1700 1710 1720 1730 1740 ALARHLRAEL AVDEASPADA VLAGLAGLEA AIAAAGAPDG DRITARLREL LKAAEAAEAR 1750 1760 PGTSGDLDTA SDEELFALVD GLD

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 AAC01712.2.
[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 AAC01712.2.
[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 AAC01712.2.
[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 AAC01712.2.
[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 CAA11037.1.
[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 AAC01712.2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF040570 Genomic DNA. Translation: AAC01712.2. AJ223012 Genomic DNA. Translation: CAA11037.1.
PIR	T17465.
3D structure databases
HSSP	HSSP built from PDB template 1NM2 based on UniProtKB P72391.
ProteinModelPortal	O52790.
SMR	O52790. Positions 7-894, 1600-1690.
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. 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. 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. 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

O52790_AMYMD

Accession

Primary (citable) accession number: O52790
Secondary accession number(s): O52546

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 1998
Last sequence update:	June 1, 1998
Last modified:	December 14, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)