OXYT_STRRM
ID OXYT_STRRM Reviewed; 344 AA.
AC Q3S8P6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=N,N-dimethyltransferase OxyT {ECO:0000303|PubMed:18422316};
DE EC=2.1.1.335 {ECO:0000269|PubMed:18422316};
DE AltName: Full=4-amino-anhydrotetracycline N(4)-methyltransferase {ECO:0000305|PubMed:18422316};
DE AltName: Full=S-adenosylmethionine: dedimethylamino-4-aminoanhydrotetracycline N-methyltransferase {ECO:0000303|PubMed:1134373};
DE AltName: Full=SAM-dependent methyltransferase {ECO:0000305};
GN Name=oxyT {ECO:0000303|PubMed:16597959};
OS Streptomyces rimosus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16597959; DOI=10.1128/aem.72.4.2573-2580.2006;
RA Zhang W., Ames B.D., Tsai S.C., Tang Y.;
RT "Engineered biosynthesis of a novel amidated polyketide, using the
RT malonamyl-specific initmguPCPB_SPHCRiation module from the oxytetracycline
RT polyketide synthase.";
RL Appl. Environ. Microbiol. 72:2573-2580(2006).
RN [2]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=1134373; DOI=10.1016/0076-6879(75)43122-6;
RA Miller P.A., Hash J.H.;
RT "S-adenosylmethionine:dedimethylamino-4-aminoanhydrotetracycline N-
RT methyltransferase.";
RL Methods Enzymol. 43:603-606(1975).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=18422316; DOI=10.1021/ja800951e;
RA Zhang W., Watanabe K., Cai X., Jung M.E., Tang Y., Zhan J.;
RT "Identifying the minimal enzymes required for anhydrotetracycline
RT biosynthesis.";
RL J. Am. Chem. Soc. 130:6068-6069(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the tetracycline antibiotic,
CC oxytetracycline. Catalyzes the dimethylation of 4-amino-4-
CC de(dimethylamino)anhydrotetracycline (4-amino-ATC) to yield
CC anhydrotetracycline (ATC) (PubMed:1134373, PubMed:18422316). Also able
CC to catalyze the dimethylation of 7-chloro-, 6-demethyl-, 2-
CC decarboxamido-2-nitrile-, and 4-methylamino-derivatives of 4-amino-4-
CC de(dimethylamino)anhydrotetracycline (PubMed:1134373).
CC {ECO:0000269|PubMed:1134373, ECO:0000269|PubMed:18422316}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-dedimethylamino-anhydrotetracycline + S-adenosyl-L-
CC methionine = 4-methylamino-4-dedimethylamino-anhydrotetracycline +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50764,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:133696, ChEBI:CHEBI:133697; EC=2.1.1.335;
CC Evidence={ECO:0000269|PubMed:18422316};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylamino-4-dedimethylamino-anhydrotetracycline + S-
CC adenosyl-L-methionine = anhydrotetracycline + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:50768, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58032, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:133696; EC=2.1.1.335;
CC Evidence={ECO:0000269|PubMed:18422316};
CC -!- PATHWAY: Antibiotic biosynthesis; oxytetracycline biosynthesis.
CC {ECO:0000305|PubMed:18422316}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce the
CC tetracycline intermediate anhydrotetracycline (ATC).
CC {ECO:0000269|PubMed:18422316}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; DQ143963; AAZ78343.1; -; Genomic_DNA.
DR RefSeq; WP_003981037.1; NZ_SADA01000149.1.
DR AlphaFoldDB; Q3S8P6; -.
DR SMR; Q3S8P6; -.
DR GeneID; 66859919; -.
DR KEGG; ag:AAZ78343; -.
DR OMA; NTNHGEL; -.
DR BRENDA; 2.1.1.335; 6084.
DR UniPathway; UPA00926; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF16864; Dimerisation2; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..344
FT /note="N,N-dimethyltransferase OxyT"
FT /id="PRO_0000442358"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231..233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 344 AA; 37376 MW; A1438045D1D14B48 CRC64;
MTTTPLAPVA QARSLLQLTT AYHQAKALHS AVELGLFDLL ADGPATAEEV KDRLRIVHPL
AKEFLDALVA LELLEADGDR YRNSPAAQAF LVSGASEYLG GTVLQHARKH YHVWAGLTTA
LQEGEAGSGA EAHGPEAYPK HYEDPERARQ VMAHFDTFSS FTAEELARRV DWSGYGSFID
IGGARGNLAT RVALAHPHLH GAVFDLPALA PLAGELIRER GLEGRVRFHG GDFLTDPLPS
ADAVVTGHVL PDWPVPQRRK LLARIHEALP SGGALVVYDL MTDPATTTVH DVLQRLNHGL
IRGDSSSSSV EEYRAEIEEA GFRVRQAERI DNLLGDWLIV AVKP
