ID   MRSA_PSESY              Reviewed;         350 AA.
AC   D5FKJ3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=2-ketoarginine methyltransferase;
DE            EC=2.1.1.243;
GN   Name=mrsA;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=22d/93;
RX   PubMed=20190091; DOI=10.1128/aem.00666-09;
RA   Braun S.D., Hofmann J., Wensing A., Ullrich M.S., Weingart H., Volksch B.,
RA   Spiteller D.;
RT   "Identification of the biosynthetic gene cluster for 3-methylarginine, a
RT   toxin produced by Pseudomonas syringae pv. syringae 22d/93.";
RL   Appl. Environ. Microbiol. 76:2500-2508(2010).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase involved
CC       in the formation of 3-methylarginine (MeArg), a potent antibiotic
CC       against the closely related soybean pathogen P.syringae pv. glycinea.
CC       Transfers the methyl group from S-adenosyl-L-methionine into 5-
CC       guanidino-2-oxopentanoate acid to yield 5-guanidino-3-methyl-2-
CC       oxopentanoate5-guanidino-3-methyl-2-oxopentanoate, a precursor of
CC       MeArg. {ECO:0000269|PubMed:20190091}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-guanidino-2-oxopentanoate + S-adenosyl-L-methionine = 5-
CC         guanidino-3-methyl-2-oxopentanoate + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:32663, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58489, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64263; EC=2.1.1.243;
CC         Evidence={ECO:0000269|PubMed:20190091};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7 mM for 5-guanidino-2-oxopentanoate
CC         {ECO:0000269|PubMed:20190091};
CC         Note=kcat is 85 min(-1).;
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:20190091}.
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DR   EMBL; FJ788104; ACY54549.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5FKJ3; -.
DR   SMR; D5FKJ3; -.
DR   BRENDA; 2.1.1.243; 5193.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030899; MrsA.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR04543; ketoArg_3Met; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..350
FT                   /note="2-ketoarginine methyltransferase"
FT                   /id="PRO_0000418454"
SQ   SEQUENCE   350 AA;  38734 MW;  2262207018B7AF19 CRC64;
     MNLLDSIKSE NTGFETTLIK GIEPIRQFVL AISIYHLFDT KLFSLLIKHE VASPEVACNE
     LGMEKEKLLG LFRYLKNEGI LLETIDGFSL SKEGHALAPF EGWYVMLVGG YATTFLQMGE
     RLQEGAGWAT RDATKVGVGS CGISHFDAIP LTRSLMAQAP GTCTKLLDLG CGNGRYLAEF
     CKALPQIQAW GAEPDRGGFE EAVDLIEKEG LSHRVHISHS GAVEFLDSDF DFEPDFIVLG
     FVLHEILGQA GRPAVVNFLK KIVHRFPAIN LIIIEVDNQF DNAGAMRHGL ALAYYNPYYL
     LHCFTNQLLV QDADWLDIFA EAGLSLVTRE TTSDQVDSTG LEIGYLLRRA