RIFG_AMYMS
ID RIFG_AMYMS Reviewed; 351 AA.
AC G0FS62; O52549;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Putative aminodehydroquinate synthase {ECO:0000305|PubMed:11278540};
DE Short=aDHQS {ECO:0000303|PubMed:11278540};
DE EC=4.2.3.- {ECO:0000305|PubMed:11278540};
GN Name=rifG {ECO:0000303|PubMed:9512878};
GN OrderedLocusNames=RAM_03190 {ECO:0000312|EMBL:AEK39130.1};
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 FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: May catalyze the conversion of 3,4-dideoxy-4-amino-D-arabino-
CC heptulosonate 7-phosphate (aDAHP) to 5-deoxy-5-amino-3-dehydroquinate
CC (aDHQ). Probably involved in the formation of 3-amino-5-hydroxybenzoic
CC acid (AHBA), the precursor of rifamycin and related ansamycins.
CC {ECO:0000305|PubMed:11278540}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q3M6C3};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q3M6C3};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q3M6C3};
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene does not affect
CC rifamycin production significantly. {ECO:0000269|PubMed:11278540}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. aDHQS
CC family. {ECO:0000305}.
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DR EMBL; AF040570; AAC01717.1; -; Genomic_DNA.
DR EMBL; CP002896; AEK39130.1; -; Genomic_DNA.
DR RefSeq; WP_013222554.1; NC_018266.1.
DR AlphaFoldDB; G0FS62; -.
DR SMR; G0FS62; -.
DR STRING; 713604.RAM_03190; -.
DR EnsemblBacteria; AEK39130; AEK39130; RAM_03190.
DR KEGG; amn:RAM_03190; -.
DR PATRIC; fig|713604.12.peg.663; -.
DR OMA; ARAHFIG; -.
DR OrthoDB; 1677032at2; -.
DR BioCyc; MetaCyc:MON-20728; -.
DR Proteomes; UP000006138; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt; Lyase;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..351
FT /note="Putative aminodehydroquinate synthase"
FT /id="PRO_0000441287"
FT BINDING 65..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 97..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 121..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 161..164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT CONFLICT 143
FT /note="K -> E (in Ref. 1; AAC01717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 36930 MW; 79E9BC92005BCDED CRC64;
MRTTIPVRLA ERSYDVLVGP GVRAALPEVV RRLGARRAVV VSARPADWVP GTGVETLLLQ
ARDGEPTKRL STVEELCGEF ARFGLTRSDV VVSCGGGTTT DVVGLAAALY HRGVAVVHLP
TSLLAQVDAS VGGKTAVNLP AGKNLVGAYW QPSAVLCDTD YLTTLPRREV LNGLGEIARC
HFIGAPDLRG RSRPEQIAAS VTLKAGIVAQ DERDTGPRHL LNYGHTLGHA LEIATGFALR
HGEAVAIGTV FAGRLAGALG RLDQSGVDEH LAVVRHYGLP AALPADVDPA VLVRQMYRDK
KAITGLAFVL AGPRGAELVS DVPAPVVTDV LDRMPRDSLE NLVGTTEAAA P
