RIFL_AMYMS
ID RIFL_AMYMS Reviewed; 358 AA.
AC Q7BUE1; G0FS66;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Putative UDP-kanosamine synthase oxidoreductase subunit;
DE EC=1.1.1.-;
DE AltName: Full=UDP-glucose 3-dehydrogenase;
GN Name=rifL; OrderedLocusNames=RAM_03210, AMES_0626;
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 DISRUPTION PHENOTYPE, AND ROLE IN RIFAMYCIN BIOSYNTHESIS.
RC STRAIN=S699;
RX PubMed=11278540; DOI=10.1074/jbc.m009667200;
RA Yu T.W., Muller R., Muller M., Zhang X., Draeger G., Kim C.G., Leistner E.,
RA Floss H.G.;
RT "Mutational analysis and reconstituted expression of the biosynthetic genes
RT involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter
RT unit of rifamycin biosynthesis in amycolatopsis Mediterranei S699.";
RL J. Biol. Chem. 276:12546-12555(2001).
RN [5]
RP PUTATIVE FUNCTION AS UDP-GLUCOSE DEHYDROGENASE, PATHWAY, AND INTERACTION
RP WITH RIFK.
RC STRAIN=S699;
RX PubMed=21081954; DOI=10.1038/ja.2010.139;
RA Floss H.G., Yu T.W., Arakawa K.;
RT "The biosynthesis of 3-amino-5-hydroxybenzoic acid (AHBA), the precursor of
RT mC7N units in ansamycin and mitomycin antibiotics: a review.";
RL J. Antibiot. 64:35-44(2011).
CC -!- FUNCTION: In a complex with RifK, RifL may catalyze the oxidation of
CC UDP-glucose to UDP-3-keto-D-glucose, which would then be used by RifK
CC to produce UDP-kanosamine. Is not able to use dTDP-glucose as
CC substrate. {ECO:0000269|PubMed:11278540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + UDP-alpha-D-glucose = H(+) + NADH + UDP-3-oxo-alpha-
CC D-glucose; Xref=Rhea:RHEA:35755, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:71965;
CC -!- PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis.
CC {ECO:0000269|PubMed:21081954}.
CC -!- SUBUNIT: Interacts with RifK. {ECO:0000269|PubMed:21081954}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC rifamycin B, but production can be restored to wild-type levels by
CC supplementation of the culture with 3-amino-5-hydroxybenzoate (AHBA).
CC {ECO:0000269|PubMed:11278540}.
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DR EMBL; AF040570; AAS07754.1; -; Genomic_DNA.
DR EMBL; CP002896; AEK39134.1; -; Genomic_DNA.
DR EMBL; CP003729; AFO74162.1; -; Genomic_DNA.
DR RefSeq; WP_013222558.1; NC_018266.1.
DR AlphaFoldDB; Q7BUE1; -.
DR SMR; Q7BUE1; -.
DR STRING; 713604.RAM_03210; -.
DR EnsemblBacteria; AEK39134; AEK39134; RAM_03210.
DR KEGG; amm:AMES_0626; -.
DR KEGG; amn:RAM_03210; -.
DR PATRIC; fig|713604.12.peg.667; -.
DR HOGENOM; CLU_023194_1_4_11; -.
DR OMA; PGSWFTD; -.
DR OrthoDB; 1465613at2; -.
DR BioCyc; MetaCyc:MON-14077; -.
DR UniPathway; UPA01029; -.
DR Proteomes; UP000006138; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0102982; F:UDP-3-dehydro-alpha-D-glucose dehydrogenase activity; IEA:RHEA.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..358
FT /note="Putative UDP-kanosamine synthase oxidoreductase
FT subunit"
FT /id="PRO_0000422401"
SQ SEQUENCE 358 AA; 37933 MW; 93D1D961AD3FFE27 CRC64;
MSVRAAVVGL GWAGRELWLP LLREHADFEV VAAVDADPAS RQAFTKATGI PTHAAVSALT
AREVDLAVVA VPNYLHTEVA GALLATGISV FLEKPVCLNS AEIDVLAAAE RSGGMLLAGS
AARYRGDVGA LRRLLPELGE IRHVALGWIR ARGVPRAGGW FTQREKAGGG ALYDLGWHLL
DTLAFLLGPA AFTQVIGVTS DDFVNAGAWR AAWRQDQLGA DAADVEDTAR GFLVRDDGVS
VSLRASWASH QARDVSVIHV EGSAGTADLR CTFGFSPNRE PEPVLSVTRE GTTTRLPVPL
ERIGVEYTRQ VSDLAAMLAD PGHRGRAVAE ARPIVSMIEN FYASAGSARG RGAVPAYQ
