ID   CMOA_NITSB              Reviewed;         239 AA.
AC   A6Q429;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=NIS_1129;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF70238.1; -; Genomic_DNA.
DR   RefSeq; WP_012082501.1; NC_009662.1.
DR   AlphaFoldDB; A6Q429; -.
DR   SMR; A6Q429; -.
DR   STRING; 387092.NIS_1129; -.
DR   EnsemblBacteria; BAF70238; BAF70238; NIS_1129.
DR   KEGG; nis:NIS_1129; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_078475_0_0_7; -.
DR   OMA; MIELYYL; -.
DR   OrthoDB; 1739932at2; -.
DR   Proteomes; UP000001118; 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..239
FT                   /note="Carboxy-S-adenosyl-L-methionine synthase"
FT                   /id="PRO_0000314348"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         61..63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         111..112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ   SEQUENCE   239 AA;  27674 MW;  85D326D61BC1BC74 CRC64;
     MEKDKVFAKP IEKRFEFDEE VASVFDDMIA RSVPFYKENM ALVRDIVVKN VVQKDRVYDL
     GCSTGSLLID IAKRSPFSLE LIGLDSSEAM LQRAHHKAKA FGVSIDFQKA DIISYAYKPA
     KIFISNYTLQ FIRPLKREPL VQKIYDALVD EGIFVFSEKV ISADKTLDKQ LLDIYFDFKK
     KQGYSDFEIA QKREALENVL VPYTLEENME MVKKCGFGFV EPIFRWANFV TFVAIKRKK