ID   CMOA_HAMD5              Reviewed;         255 AA.
AC   C4K5W2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=HDEF_1305;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001277; ACQ67955.1; -; Genomic_DNA.
DR   RefSeq; WP_015873744.1; NC_012751.1.
DR   AlphaFoldDB; C4K5W2; -.
DR   SMR; C4K5W2; -.
DR   STRING; 572265.HDEF_1305; -.
DR   EnsemblBacteria; ACQ67955; ACQ67955; HDEF_1305.
DR   GeneID; 66260999; -.
DR   KEGG; hde:HDEF_1305; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_078475_0_0_6; -.
DR   OMA; MIELYYL; -.
DR   Proteomes; UP000002334; 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..255
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_1000215638"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         70..72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         124..125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         139
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   255 AA;  28931 MW;  E198857E56C34BC0 CRC64;
     MVLSSKNDQP DHLFAAPIEK LGDWAFDEQV AAVFPNMITR SIPGYTNIIT MIGMLSKRFV
     KPHTQIYDLG CSHGAACLSI YPNILDIPSC KIIAVEESPA MIKYCRENLM AHCDQIPIEI
     IEDDILNIKI DNASMVILNF TLQFLDPGHR ENVLNRIYQG LNPGGILVLS EKFHFEDPDI
     GPLLFDMHHD FKRAHGYSDL EISQKSTMLK NVMRIDSVET HQNRLRQAGF EQMDLWFQCF
     NFGSLLALKT SSSND