CMOA_ECOLI
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 03-AUG-2022, entry version 158.
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, ECO:0000303|PubMed:23676670,
GN ECO:0000303|PubMed:23695253}; Synonyms=yecO;
GN OrderedLocusNames=b1870, JW1859;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (1.73 ANGSTROMS) OF 19-247 IN COMPLEX WITH
RP CARBOXY-S-ADENOSYL-METHIONINE, AND 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 (1.50 ANGSTROMS) IN COMPLEX WITH
RP CARBOXY-S-ADENOSYL-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND
RP 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 = 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, 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_SSZK01000001.1.
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 PDBsum; 4GEK; -.
DR PDBsum; 4IWN; -.
DR AlphaFoldDB; P76290; -.
DR SMR; P76290; -.
DR BioGRID; 4263500; 34.
DR IntAct; P76290; 6.
DR MINT; P76290; -.
DR STRING; 511145.b1870; -.
DR SWISS-2DPAGE; P76290; -.
DR jPOST; P76290; -.
DR PaxDb; P76290; -.
DR PRIDE; P76290; -.
DR EnsemblBacteria; AAC74940; AAC74940; b1870.
DR EnsemblBacteria; BAA15680; BAA15680; BAA15680.
DR GeneID; 946380; -.
DR KEGG; ecj:JW1859; -.
DR KEGG; eco:b1870; -.
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; MIELYYL; -.
DR PhylomeDB; P76290; -.
DR BioCyc; EcoCyc:G7020-MON; -.
DR BioCyc; MetaCyc:G7020-MON; -.
DR BRENDA; 2.1.1.229; 2026.
DR PRO; PR:P76290; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IMP:EcoCyc.
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 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..76
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
