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Database: UniProt
Entry: RIFF_AMYMD
LinkDB: RIFF_AMYMD
Original site: RIFF_AMYMD 
ID   RIFF_AMYMD              Reviewed;         260 AA.
AC   O52547;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   19-JAN-2010, entry version 43.
DE   RecName: Full=3-amino-5-hydroxybenzoic acid synthase;
DE            Short=AHBA synthase;
DE            EC=2.3.1.-;
DE   AltName: Full=Rifamycin amide synthase;
GN   Name=rifF;
OS   Amycolatopsis mediterranei (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=33910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
CC   -!- FUNCTION: Putatively terminates polyketide biosynthesis by
CC       transfer of polyketide acyl chain to the secondary amine on the 3-
CC       AHBA starter unit.
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
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DR   EMBL; AF040570; AAC01715.1; -; Genomic_DNA.
DR   SMR; O52547; 4-254.
DR   BioCyc; MetaCyc:MONOMER-14108; -.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR001447; N-AcTrfase.
DR   PANTHER; PTHR11786; Acetyltransf2; 1.
DR   Pfam; PF00797; Acetyltransf_2; 1.
DR   PRINTS; PR01543; ANATRNSFRASE.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN         1    260       3-amino-5-hydroxybenzoic acid synthase.
FT                                /FTId=PRO_0000107920.
FT   ACT_SITE     73     73       Acyl-thioester intermediate (By
FT                                similarity).
FT   ACT_SITE    111    111       By similarity.
FT   ACT_SITE    126    126       By similarity.
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
//
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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (1)   
   Pfam (1)   
   PRINTS (1)   
Literature (1)   
   PubMed (1)   
All databases (8)   
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