NOVP_STRNV
ID NOVP_STRNV Reviewed; 262 AA.
AC Q9L9F2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Demethyldecarbamoylnovobiocin O-methyltransferase {ECO:0000305};
DE EC=2.1.1.285 {ECO:0000269|PubMed:14694473};
DE AltName: Full=Novobiocin biosynthesis protein P;
GN Name=novP;
OS Streptomyces niveus (Streptomyces spheroides).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=193462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT spheroides NCIB 11891.";
RL Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX PubMed=14694473; DOI=10.1002/anie.200352626;
RA Freel Meyers C.L., Oberthur M., Xu H., Heide L., Kahne D., Walsh C.T.;
RT "Characterization of NovP and NovN: completion of novobiocin biosynthesis
RT by sequential tailoring of the noviosyl ring.";
RL Angew. Chem. Int. Ed. 43:67-70(2004).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX PubMed=15218104; DOI=10.1073/pnas.0403526101;
RA Pi N., Meyers C.L., Pacholec M., Walsh C.T., Leary J.A.;
RT "Mass spectrometric characterization of a three-enzyme tandem reaction for
RT assembly and modification of the novobiocin skeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10036-10041(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, AND SUBUNIT.
RX PubMed=19857499; DOI=10.1016/j.jmb.2009.10.045;
RA Gomez Garcia I., Stevenson C.E., Uson I., Freel Meyers C.L., Walsh C.T.,
RA Lawson D.M.;
RT "The crystal structure of the novobiocin biosynthetic enzyme NovP: the
RT first representative structure for the TylF O-methyltransferase
RT superfamily.";
RL J. Mol. Biol. 395:390-407(2010).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent O-methyltransferase that
CC methylates at 4-OH of the noviose moiety, the penultimate step in the
CC novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family
CC antibiotic that targets bacterial DNA gyrases.
CC {ECO:0000269|PubMed:14694473, ECO:0000269|PubMed:15218104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=desmethyldescarbamoylnovobiocin + S-adenosyl-L-methionine =
CC descarbamoylnovobiocin + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36655, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:73955, ChEBI:CHEBI:73957;
CC EC=2.1.1.285; Evidence={ECO:0000269|PubMed:14694473};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 uM for demethyldecarbamoylnovobiocin
CC {ECO:0000269|PubMed:14694473};
CC Note=kcat is 0.4 min(-1) with demethyldecarbamoylnovobiocin as
CC substrate.;
CC -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC {ECO:0000269|PubMed:14694473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19857499}.
CC -!- SIMILARITY: Belongs to the methyltransferase TylF/MycF family.
CC {ECO:0000305}.
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DR EMBL; AF170880; AAF67509.1; -; Genomic_DNA.
DR RefSeq; WP_069626145.1; NZ_MDCR01000039.1.
DR PDB; 2WK1; X-ray; 1.40 A; A=1-262.
DR PDBsum; 2WK1; -.
DR AlphaFoldDB; Q9L9F2; -.
DR SMR; Q9L9F2; -.
DR KEGG; ag:AAF67509; -.
DR BioCyc; MetaCyc:MON-18053; -.
DR BRENDA; 2.1.1.285; 6099.
DR UniPathway; UPA01035; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:0043642; P:novobiocin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR008884; TylF_MeTrfase.
DR PANTHER; PTHR40036; PTHR40036; 1.
DR Pfam; PF05711; TylF; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Magnesium; Metal-binding;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..262
FT /note="Demethyldecarbamoylnovobiocin O-methyltransferase"
FT /id="PRO_0000424004"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 92..96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 122..126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 196..197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19857499"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2WK1"
FT TURN 27..32
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:2WK1"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2WK1"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2WK1"
SQ SEQUENCE 262 AA; 29967 MW; 2FC79BADAC4E0184 CRC64;
MAPIVETAKE TNSDSSLYLD LMIKVLAGTV YEDPAHRENF SHRDSTYREE VRNEGRDWPA
NAHTMIGIKR LENIRQCVED VIGNNVPGDL VETGVWRGGA CILMRGILRA HDVRDRTVWV
ADSFQGIPDV GEDGYAGDRK MALHRRNSVL AVSEEEVRRN FRNYDLLDEQ VRFLPGWFKD
TLPTAPIDTL AVLRMDGDLY ESTWDTLTNL YPKVSVGGYV IVDDYMMCPP CKDAVDEYRA
KFDIADELIT IDRDGVYWQR TR
