ID   CMOA_ECOLI              Reviewed;         247 AA.
AC   P76290; O07982;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 176.
DE   RecName: Full=Carboxy-S-adenosyl-L-methionine synthase {ECO:0000255|HAMAP-Rule:MF_01589, ECO:0000305};
DE            Short=Cx-SAM synthase {ECO:0000255|HAMAP-Rule:MF_01589, ECO:0000303|PubMed:23676670};
DE            EC=2.1.3.- {ECO:0000255|HAMAP-Rule:MF_01589, ECO:0000269|PubMed:23676670};
GN   Name=cmoA {ECO:0000255|HAMAP-Rule:MF_01589,
GN   ECO:0000303|PubMed:23676670, ECO:0000303|PubMed:23695253};
GN   Synonyms=yecO; OrderedLocusNames=b1870, JW1859;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4] {ECO:0007744|PDB:4IWN}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE, AND
RP   SUBUNIT.
RX   PubMed=23695253; DOI=10.1107/s0907444913004939;
RA   Byrne R.T., Whelan F., Aller P., Bird L.E., Dowle A., Lobley C.M.,
RA   Reddivari Y., Nettleship J.E., Owens R.J., Antson A.A., Waterman D.G.;
RT   "S-adenosyl-S-carboxymethyl-L-homocysteine: a novel cofactor found in the
RT   putative tRNA-modifying enzyme CmoA.";
RL   Acta Crystallogr. D 69:1090-1098(2013).
RN   [5] {ECO:0007744|PDB:4GEK}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE,
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-89.
RX   PubMed=23676670; DOI=10.1038/nature12180;
RA   Kim J., Xiao H., Bonanno J.B., Kalyanaraman C., Brown S., Tang X.,
RA   Al-Obaidi N.F., Patskovsky Y., Babbitt P.C., Jacobson M.P., Lee Y.S.,
RA   Almo S.C.;
RT   "Structure-guided discovery of the metabolite carboxy-SAM that modulates
RT   tRNA function.";
RL   Nature 498:123-126(2013).
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, ECO:0000269|PubMed:23676670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + S-adenosyl-L-methionine = carboxy-S-adenosyl-L-
CC         methionine + 3-phenylpyruvate + 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, ECO:0000269|PubMed:23676670};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01589,
CC       ECO:0000269|PubMed:23695253}.
CC   -!- MISCELLANEOUS: Mechanistic analyses show the involvement of a unique
CC       ylide intermediate as the carboxyl acceptor in the conversion of SAM to
CC       Cx-SAM. {ECO:0000269|PubMed:23676670}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cx-SAM synthase family. {ECO:0000255|HAMAP-Rule:MF_01589,
CC       ECO:0000305}.
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DR   EMBL; U00096; AAC74940.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15680.1; -; Genomic_DNA.
DR   PIR; F64949; F64949.
DR   RefSeq; NP_416384.1; NC_000913.3.
DR   RefSeq; WP_000019590.1; NZ_CP009789.1.
DR   PDB; 4GEK; X-ray; 1.50 A; A/G=1-247.
DR   PDB; 4IWN; X-ray; 1.73 A; A/B=19-247.
DR   SMR; P76290; -.
DR   BioGRID; 4263500; 40.
DR   IntAct; P76290; 6.
DR   STRING; 511145.b1870; -.
DR   PaxDb; 511145-b1870; -.
DR   jPOST; P76290; -.
DR   EnsemblBacteria; AAC74940; AAC74940; b1870.
DR   GeneID; 946380; -.
DR   KEGG; ecj:JW1859; -.
DR   KEGG; eco:b1870; -.
DR   KEGG; ecoc:C3026_10645; -.
DR   PATRIC; fig|1411691.4.peg.378; -.
DR   EchoBASE; EB3787; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_078475_0_0_6; -.
DR   InParanoid; P76290; -.
DR   OMA; ACAVQWT; -.
DR   OrthoDB; 9779941at2; -.
DR   PhylomeDB; P76290; -.
DR   BioCyc; EcoCyc:G7020-MONOMER; -.
DR   BioCyc; MetaCyc:G7020-MONOMER; -.
DR   BRENDA; 2.1.1.229; 2026.
DR   EvolutionaryTrace; P76290; -.
DR   PRO; PR:P76290; -.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000030; Carboxy-S-adenosyl-L-methionine synthase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; CARBOXY-S-ADENOSYL-L-METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   PIRSF; PIRSF006325; MeTrfase_bac; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   NCBIfam; TIGR00740; carboxy-S-adenosyl-L-methionine synthase CmoA; 1.
DR   NCBIfam; NF011995; cmoA; 1.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IMP:EcoCyc.
DR   Proteomes; UP000000625; Chromosome.
DR   AlphaFoldDB; P76290; -.
DR   FunCoup; P76290; 84.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..247
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000169083"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
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                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
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                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
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                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT                   ECO:0000269|PubMed:23676670, ECO:0000269|PubMed:23695253"
FT   MUTAGEN         89
FT                   /note="D->L: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:23676670"
FT   HELIX           20..35
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           69..75
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           92..103
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          111..116
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          125..133
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           140..153
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          154..166
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           171..187
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           196..203
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   HELIX           211..221
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          224..232
FT                   /evidence="ECO:0007829|PDB:4IWN"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:4IWN"
SQ   SEQUENCE   247 AA;  27777 MW;  2930565435F5A7F4 CRC64;
     MSHRDTLFSA PIARLGDWTF DERVAEVFPD MIQRSVPGYS NIISMIGMLA ERFVQPGTQV
     YDLGCSLGAA TLSVRRNIHH DNCKIIAIDN SPAMIERCRR HIDAYKAPTP VDVIEGDIRD
     IAIENASMVV LNFTLQFLEP SERQALLDKI YQGLNPGGAL VLSEKFSFED AKVGELLFNM
     HHDFKRANGY SELEISQKRS MLENVMLTDS VETHKARLHN AGFEHSELWF QCFNFGSLVA
     LKAEDAA
//