RIFF_AMYMS
ID RIFF_AMYMS Reviewed; 260 AA.
AC O52547; G0FS60;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Proansamycin X synthase;
DE EC=4.4.1.-;
DE AltName: Full=Rifamycin amide synthase;
GN Name=rifF; OrderedLocusNames=RAM_03180, AMES_0620;
OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=713604;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=9512878; DOI=10.1016/s1074-5521(98)90141-7;
RA August P.R., Tang L., Yoon Y.J., Ning S., Mueller R., Yu T.W., Taylor M.,
RA Hoffmann D., Kim C.G., Zhang X., Hutchinson C.R., Floss H.G.;
RT "Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the
RT molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis
RT mediterranei S699.";
RL Chem. Biol. 5:69-79(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=21914879; DOI=10.1128/jb.05819-11;
RA Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT "Whole genome sequence of the rifamycin B-producing strain Amycolatopsis
RT mediterranei S699.";
RL J. Bacteriol. 193:5562-5563(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=23012281; DOI=10.1128/jb.01295-12;
RA Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.;
RT "Complete genome sequence of Amycolatopsis mediterranei S699 based on de
RT novo assembly via a combinatorial sequencing strategy.";
RL J. Bacteriol. 194:5699-5700(2012).
RN [4]
RP PROTEIN SEQUENCE OF 1-10, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP 3D-STRUCTURE MODELING.
RC STRAIN=S699;
RX PubMed=11812235; DOI=10.1006/prep.2001.1550;
RA Pompeo F., Mushtaq A., Sim E.;
RT "Expression and purification of the rifamycin amide synthase, RifF, an
RT enzyme homologous to the prokaryotic arylamine N-acetyltransferases.";
RL Protein Expr. Purif. 24:138-151(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=N/813;
RX PubMed=10627035; DOI=10.1099/00221287-145-12-3365;
RA Stratmann A., Toupet C., Schilling W., Traber R., Oberer L., Schupp T.;
RT "Intermediates of rifamycin polyketide synthase produced by an
RT Amycolatopsis mediterranei mutant with inactivated rifF gene.";
RL Microbiology 145:3365-3375(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=S699;
RX PubMed=10430893; DOI=10.1073/pnas.96.16.9051;
RA Yu T.W., Shen Y., Doi-Katayama Y., Tang L., Park C., Moore B.S.,
RA Richard Hutchinson C., Floss H.G.;
RT "Direct evidence that the rifamycin polyketide synthase assembles
RT polyketide chains processively.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9051-9056(1999).
CC -!- FUNCTION: Catalyzes the release of the completed linear polyketide from
CC the rif PKS by forming an intramolecular amide bond, in this way
CC terminating polyketide assembly and forming the macrocyclic compound
CC proansamycin X, an intermediate in the rifamycin B biosynthesis.
CC {ECO:0000269|PubMed:10430893, ECO:0000269|PubMed:10627035}.
CC -!- PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis.
CC -!- DISRUPTION PHENOTYPE: Inactivation of rifF gives a rifamycin B non-
CC producing mutant that still accumulates a series of linear polyketides
CC ranging from the tetra- to a decaketide, also detected in the wild-
CC type. {ECO:0000269|PubMed:10430893, ECO:0000269|PubMed:10627035}.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF040570; AAC01715.1; -; Genomic_DNA.
DR EMBL; CP002896; AEK39128.1; -; Genomic_DNA.
DR EMBL; CP003729; AFO74156.1; -; Genomic_DNA.
DR RefSeq; WP_013222552.1; NC_018266.1.
DR AlphaFoldDB; O52547; -.
DR SMR; O52547; -.
DR STRING; 713604.RAM_03180; -.
DR EnsemblBacteria; AEK39128; AEK39128; RAM_03180.
DR KEGG; amm:AMES_0620; -.
DR KEGG; amn:RAM_03180; -.
DR PATRIC; fig|713604.12.peg.661; -.
DR HOGENOM; CLU_049918_1_0_11; -.
DR OMA; NAWALED; -.
DR OrthoDB; 1687886at2; -.
DR BioCyc; MetaCyc:MON-14108; -.
DR UniPathway; UPA01029; -.
DR Proteomes; UP000006138; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001447; Arylamine_N-AcTrfase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR11786; PTHR11786; 1.
DR Pfam; PF00797; Acetyltransf_2; 1.
DR PRINTS; PR01543; ANATRNSFRASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Direct protein sequencing; Lyase;
KW Reference proteome.
FT CHAIN 1..260
FT /note="Proansamycin X synthase"
FT /id="PRO_0000107920"
FT ACT_SITE 73
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 29192 MW; C32605EBC0BFBF47 CRC64;
MNVFDVETYL QRIGCGGETG VDLETLAKLQ KSHLMAIPYS SLAYELRDAV NVVDLDEDDV
FVTSIAEGQG GACYHLNRLF HRLLTELGYD VTPLAGSTAE GRETFGTDVE HMFNLVTLDG
ADWLVDVGYP GPTYVEPLAV SPAVQTQYGS QFRLVEQETG YALQRRGAVT RWSVVYTFTT
QPRQWSDWKE LEDNFRALVG DTTRTDTQET LCGRAFANGQ VFLRQRRYLT VENGREQVRT
ITDDDEFRAL VSRVLSGDHG
