MPPJ_STRHY
ID MPPJ_STRHY Reviewed; 337 AA.
AC Q643C8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Phenylpyruvate C(3)-methyltransferase;
DE EC=2.1.1.281;
DE AltName: Full=Mannopeptimycin biosynthesis protein J;
GN Name=mppJ;
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16723579; DOI=10.1128/aac.01545-05;
RA Magarvey N.A., Haltli B., He M., Greenstein M., Hucul J.A.;
RT "Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics
RT active against drug-resistant gram-positive pathogens.";
RL Antimicrob. Agents Chemother. 50:2167-2177(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=NRRL 3085;
RX PubMed=19731276; DOI=10.1002/cbic.200900351;
RA Huang Y.T., Lyu S.Y., Chuang P.H., Hsu N.S., Li Y.S., Chan H.C.,
RA Huang C.J., Liu Y.C., Wu C.J., Yang W.B., Li T.L.;
RT "In vitro characterization of enzymes involved in the synthesis of
RT nonproteinogenic residue (2S,3S)-beta-methylphenylalanine in glycopeptide
RT antibiotic mannopeptimycin.";
RL ChemBioChem 10:2480-2487(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase involved
CC in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-
CC phenylalanine, a building block of the antibiotic mannopeptimycin.
CC {ECO:0000269|PubMed:19731276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + S-adenosyl-L-methionine = (3S)-2-oxo-3-
CC phenylbutanoate + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36623, ChEBI:CHEBI:15378, ChEBI:CHEBI:18005,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74119;
CC EC=2.1.1.281; Evidence={ECO:0000269|PubMed:19731276};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.014 mM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:19731276};
CC KM=2.5 mM for phenylpyruvic acid {ECO:0000269|PubMed:19731276};
CC Note=kcat is 0.8 sec(-1) with S-adenosyl-L-methionine as substrate.
CC kcat is 8.15 sec(-1) with phenylpyruvic acid as substrate.;
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19731276}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY735112; AAU34201.1; -; Genomic_DNA.
DR PDB; 4KIB; X-ray; 2.00 A; A/B=1-337.
DR PDB; 4KIC; X-ray; 2.43 A; A/B=1-337.
DR PDB; 4KIF; X-ray; 2.50 A; A/B=1-337.
DR PDB; 4KIG; X-ray; 2.40 A; A/B=1-337.
DR PDB; 4M6X; X-ray; 2.30 A; A/B=1-337.
DR PDB; 4M6Y; X-ray; 2.50 A; A/B=1-337.
DR PDB; 4M71; X-ray; 2.21 A; A/B=1-337.
DR PDB; 4M72; X-ray; 2.10 A; A/B=1-337.
DR PDB; 4M73; X-ray; 2.00 A; A/B=1-337.
DR PDB; 4M74; X-ray; 2.20 A; A/B=1-337.
DR PDBsum; 4KIB; -.
DR PDBsum; 4KIC; -.
DR PDBsum; 4KIF; -.
DR PDBsum; 4KIG; -.
DR PDBsum; 4M6X; -.
DR PDBsum; 4M6Y; -.
DR PDBsum; 4M71; -.
DR PDBsum; 4M72; -.
DR PDBsum; 4M73; -.
DR PDBsum; 4M74; -.
DR AlphaFoldDB; Q643C8; -.
DR SMR; Q643C8; -.
DR KEGG; ag:AAU34201; -.
DR BioCyc; MetaCyc:MON-18033; -.
DR BRENDA; 2.1.1.281; 6043.
DR BRENDA; 2.6.1.107; 6043.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..337
FT /note="Phenylpyruvate C(3)-methyltransferase"
FT /id="PRO_0000424006"
FT HELIX 7..33
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:4KIB"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:4KIB"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4KIB"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:4KIB"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:4KIB"
FT STRAND 318..337
FT /evidence="ECO:0007829|PDB:4KIB"
SQ SEQUENCE 337 AA; 37186 MW; DFAB6513443BB14F CRC64;
MSTEVSEAQA RRAVADIFNS TLASSAIGAA WELGALDELR ENGKLDVSDF AVRHDLHEPA
VVGMFTALAS VGIVRREGAT VVVGPYFDEA NHHRSLFHWL NQGSGELFRR MPQVLPNENR
TGKFYQRDAG AISYACREIS ERYFDPAFWA AVDGLGYTPT TVADLGSGSG ERLIQIARRF
PGVRGLGVDI ADGAIAMAEK EVAAKGFGDQ ISFVRGDART IDQVSARGEF AEVDLLTCFM
MGHDFWPREN CVQTLRKLRA AFPNVRRFLL GDATRTVGIP DRELPVFTLG FEFGHDMMGV
YLPTLDEWDG VFEEGGWRCV KKHAIDSLSV SVVFELE
