ID   CMOA_CAMJR              Reviewed;         235 AA.
AC   Q5HVI0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CJE0693;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW35797.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5HVI0; -.
DR   SMR; Q5HVI0; -.
DR   KEGG; cjr:CJE0693; -.
DR   HOGENOM; CLU_078475_0_0_7; -.
DR   OMA; MIELYYL; -.
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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43861:SF2; PTHR43861:SF2; 1.
DR   Pfam; PF13847; Methyltransf_31; 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..235
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000314315"
FT   BINDING         35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         60..62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         83..84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   235 AA;  27166 MW;  AA74958EAD6991A1 CRC64;
     MKDELFKQSP KKQFEFDKSV ASVFDDMINR SVPFYRENLE LCGNLLAKIL PTNASVCDLG
     CSSANFLIFL ANLRKDFKLF GVDNSASMLE VAKSKAKAYG LDISFFEANL CEFDFFTCDV
     FVANYTMQFI RPPKRQELLD QIYKNLNSKG ILIMSEKILY EDAFLSKNII ELYADYKEKQ
     GYSKFEIAAK REALENVLIP YSQKENLNML EKAGFKKIES IFKWANFETF IAFKD