ID   CMOA_SALTY              Reviewed;         247 AA.
AC   Q7CQC4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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, ECO:0000303|PubMed:15383682};
GN   OrderedLocusNames=STM1905;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=15383682; DOI=10.1261/rna.7106404;
RA   Naesvall S.J., Chen P., Bjoerk G.R.;
RT   "The modified wobble nucleoside uridine-5-oxyacetic acid in
RT   tRNAPro(cmo5UGG) promotes reading of all four proline codons in vivo.";
RL   RNA 10:1662-1673(2004).
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   -!- DISRUPTION PHENOTYPE: Deletion mutant shows accumulation of 5-
CC       methoxyuridine (mo5U34) and 5-hydroxyuridine (ho5U34) in tRNA.
CC       {ECO:0000269|PubMed:15383682}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cx-SAM synthase family. {ECO:0000255|HAMAP-Rule:MF_01589}.
CC   -!- CAUTION: Was originally thought to be a transferase that mediates the
CC       conversion of mo5U(34) to cmo5U(34) in tRNAs.
CC       {ECO:0000305|PubMed:15383682}.
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DR   EMBL; AE006468; AAL20821.1; -; Genomic_DNA.
DR   RefSeq; NP_460862.1; NC_003197.2.
DR   RefSeq; WP_000019609.1; NC_003197.2.
DR   AlphaFoldDB; Q7CQC4; -.
DR   SMR; Q7CQC4; -.
DR   STRING; 99287.STM1905; -.
DR   PaxDb; Q7CQC4; -.
DR   EnsemblBacteria; AAL20821; AAL20821; STM1905.
DR   GeneID; 1253426; -.
DR   KEGG; stm:STM1905; -.
DR   PATRIC; fig|99287.12.peg.2020; -.
DR   HOGENOM; CLU_078475_0_0_6; -.
DR   OMA; MIELYYL; -.
DR   PhylomeDB; Q7CQC4; -.
DR   BioCyc; SENT99287:STM1905-MON; -.
DR   Proteomes; UP000001014; 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   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..247
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000314374"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         64..66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         89..90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   247 AA;  27848 MW;  749C125C54BF19FE CRC64;
     MSHRDTLFSA PIARLGDWTF DERVAEVFPD MIQRSVPGYS NIISMIGMLA ERFVQPNTQV
     YDLGCSLGAA TLSVRRNIRH EHCRIIAVDN SPAMIERCRR HIDAYKAPTP VEVVEGDIRD
     ITIENASMVV LNFTLQFLEP AERQALLDKI YLGLNPGGAL VLSEKFSFED AKVGELLFNM
     HHDFKRANGY SELEISQKRS MLENVMLTDS VETHKARLRQ AGFEHSELWF QCFNFGSLVA
     LKAGVAA