CMOA_ECO27
ID CMOA_ECO27 Reviewed; 247 AA.
AC B7USP7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=E2348C_1995;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(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; FM180568; CAS09543.1; -; Genomic_DNA.
DR RefSeq; WP_000019589.1; NC_011601.1.
DR AlphaFoldDB; B7USP7; -.
DR SMR; B7USP7; -.
DR EnsemblBacteria; CAS09543; CAS09543; E2348C_1995.
DR KEGG; ecg:E2348C_1995; -.
DR HOGENOM; CLU_078475_0_0_6; -.
DR OMA; MIELYYL; -.
DR Proteomes; UP000008205; 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_1000185683"
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; 27821 MW; 6830565165A0A7E8 CRC64;
MSHRDTLFSA PIARLGDWTF DERVAEVFPD MIQRSVPGYS NIISMIGMLA ERFVQPGTQV
YDLGCSLGAA TLSVRRNIHH DNCKIIAIDN SPAMIERCRR HIDAYKAPTP VDVIEGDIRD
IAIENASMVV LNFTLQFLEP SERQALLDKI YQGLNPGGAL VLSEKFSFED AKVGELLFNM
HHDFKRANGY SELEISQKRS MLENVMLTDS VETHKARLHK AGFEHSELWF QCFNFGSLVT
LKAEDAA