ID   CMOA_YERPN              Reviewed;         267 AA.
AC   Q1CJH3; C4GSF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=YPN_1527;
GN   ORFNames=YP516_1695;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG17857.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000009; EEO76963.1; -; Genomic_DNA.
DR   RefSeq; WP_002211207.1; NZ_ACNQ01000009.1.
DR   AlphaFoldDB; Q1CJH3; -.
DR   SMR; Q1CJH3; -.
DR   EnsemblBacteria; ABG17857; ABG17857; YPN_1527.
DR   GeneID; 66841534; -.
DR   KEGG; ypn:YPN_1527; -.
DR   HOGENOM; CLU_078475_0_0_6; -.
DR   OMA; MIELYYL; -.
DR   Proteomes; UP000008936; 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..267
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000314408"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         84..86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         109..110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         137..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   267 AA;  30040 MW;  2B8CF18C1A21FBB9 CRC64;
     MPNRDTQSQN DTPRHSPEAA EPQRDSLFAA PIAKLGDWTF DEKVAEVFPD MIQRSVPGYS
     NIISMIGMLA ERFVQPNSQI YDLGCSLGAA TLSMRRNIKA EGCKIIAVDN SPAMVERCRR
     HIDAFRAETP VDVVEADILD IKLENASMVV LNFTLQFLEP ANRQRLLNQV YQGLRPGGAL
     VLSEKFSFAD HNVGELLFNM HHDFKRANGY SELEISQKRS MLENVMLTDS VETHKNRLHQ
     AGFEHAEVWF QCFNFGSLIA LKAGEAQ