ID   CMOA_PSEPF              Reviewed;         247 AA.
AC   Q3K7D5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Carboxy-S-adenosyl-L-methionine synthase {ECO:0000255|HAMAP-Rule:MF_01589};
DE            Short=Cx-SAM synthase {ECO:0000255|HAMAP-Rule:MF_01589};
DE            EC=2.1.3.- {ECO:0000255|HAMAP-Rule:MF_01589};
GN   Name=cmoA {ECO:0000255|HAMAP-Rule:MF_01589}; OrderedLocusNames=Pfl01_4582;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to
CC       carboxy-S-adenosyl-L-methionine (Cx-SAM). {ECO:0000255|HAMAP-
CC       Rule:MF_01589}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate +
CC         carboxy-S-adenosyl-L-methionine + H2O; Xref=Rhea:RHEA:51692,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:134278; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01589};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01589}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cx-SAM synthase family. {ECO:0000255|HAMAP-Rule:MF_01589}.
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DR   EMBL; CP000094; ABA76319.1; -; Genomic_DNA.
DR   RefSeq; WP_007956658.1; NC_007492.2.
DR   AlphaFoldDB; Q3K7D5; -.
DR   SMR; Q3K7D5; -.
DR   STRING; 205922.Pfl01_4582; -.
DR   EnsemblBacteria; ABA76319; ABA76319; Pfl01_4582.
DR   KEGG; pfo:Pfl01_4582; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_078475_0_0_6; -.
DR   OMA; MIELYYL; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01589; Cx_SAM_synthase; 1.
DR   InterPro; IPR005271; CmoA.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43861:SF2; PTHR43861:SF2; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   PIRSF; PIRSF006325; MeTrfase_bac; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00740; TIGR00740; 1.
PE   3: Inferred from homology;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..247
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000314360"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         65..67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         90..91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   247 AA;  27453 MW;  C9564476804A8B6F CRC64;
     MSKEPDRIFA QPMAQVPDFA FNEDVVRVFP DMIKRSVPGY PTIVENLGVL AAQFAQPNSV
     LYDLGASLGA VTQALRRHVR TDGCRVIAVD NSAAMVERCR EYLNGQDSMF QELLPVEVIE
     GDILALDFKP ASVVALNFTL QFIAPDQRTA LLSRIRQSLL PGGALILSEK LRFNDAEEHA
     LLTDLHVAFK RANGYSELEI AQKRSAIENV MKPDSLEEHR ERLLAAGFSK VVPWFQCLNF
     ASLIALP