CMOA_CAMJD
ID CMOA_CAMJD Reviewed; 235 AA.
AC A7H3U1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=JJD26997_1078;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
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 "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
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; CP000768; ABS44643.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H3U1; -.
DR SMR; A7H3U1; -.
DR EnsemblBacteria; ABS44643; ABS44643; JJD26997_1078.
DR KEGG; cjd:JJD26997_1078; -.
DR HOGENOM; CLU_078475_0_0_7; -.
DR OMA; MIELYYL; -.
DR Proteomes; UP000002302; 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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43861:SF2; PTHR43861:SF2; 1.
DR Pfam; PF13847; Methyltransf_31; 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..235
FT /note="Carboxy-S-adenosyl-L-methionine synthase"
FT /id="PRO_0000314316"
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 83..84
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 235 AA; 27220 MW; 6C08C92E6AD4613E CRC64;
MKDELFKQNP KKQFEFDKSV ASVFDDMINR SVPFYRENLE LCGNLLAKIL PTNASICDLG
CSSANFLIFL ANLRKDFKLF GVDNSASMLE VAKSKAKAYG LDISFFEANL CEFDFFICDV
FVANYTMQFI RPPKRQELLD KIYKNLNSKG ILIMSEKILY EDAFLSKNII ELYADYKEKQ
GYSKFEIAAK REALENVLIP YSQKENLNML EKAGFKKIES IFKWANFETF IAFKD