ID CMOA_CAMC5 Reviewed; 234 AA.
AC A7GXS7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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};
GN OrderedLocusNames=Ccur92_07150; ORFNames=CCV52592_1562;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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; CP000767; EAU00674.1; -; Genomic_DNA.
DR RefSeq; WP_011992142.1; NC_009715.2.
DR AlphaFoldDB; A7GXS7; -.
DR SMR; A7GXS7; -.
DR STRING; 360105.CCV52592_1562; -.
DR KEGG; ccv:CCV52592_1562; -.
DR HOGENOM; CLU_078475_0_0_7; -.
DR OrthoDB; 5386938at2; -.
DR Proteomes; UP000006380; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00740; carboxy-S-adenosyl-L-methionine synthase CmoA; 1.
DR PANTHER; PTHR43861:SF2; CARBOXY-S-ADENOSYL-L-METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF006325; MeTrfase_bac; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..234
FT /note="Carboxy-S-adenosyl-L-methionine synthase"
FT /id="PRO_0000381955"
FT BINDING 35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 60..62
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 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ SEQUENCE 234 AA; 26756 MW; CBF2AE42937FD5CB CRC64;
MRDEIFKEPI KKQFEFDDFV VSVFDDMIGR SVPFYDVSGK LVSEILAKIL PAKAHVIDLG
CSTATSLLLL NQLRDDLVLE GVDSSSAMIE NARKKAKAYG AKIKFSVGDV LESQICQMDA
VMMNYTLQFI RPPKRAQLVK SIYDGLNEGG VFVFSEKIIY EDKKFAKNMI EIYENYKEKQ
GYSRYEIAQK REALENVLIP YTEEENRTLA LGAGFKRVES VFKWGNFMTF LAFK
//
