CMOA_SHEON
ID CMOA_SHEON Reviewed; 243 AA.
AC Q8EEE7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SO_2435;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55469.1; -; Genomic_DNA.
DR RefSeq; NP_718025.1; NC_004347.2.
DR RefSeq; WP_011072410.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EEE7; -.
DR SMR; Q8EEE7; -.
DR STRING; 211586.SO_2435; -.
DR PaxDb; Q8EEE7; -.
DR KEGG; son:SO_2435; -.
DR PATRIC; fig|211586.12.peg.2342; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_078475_0_0_6; -.
DR OMA; MIELYYL; -.
DR OrthoDB; 1739932at2; -.
DR PhylomeDB; Q8EEE7; -.
DR BioCyc; SONE211586:G1GMP-2225-MON; -.
DR Proteomes; UP000008186; 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..243
FT /note="Carboxy-S-adenosyl-L-methionine synthase"
FT /id="PRO_0000314381"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 65..67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 90..91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 118..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
SQ SEQUENCE 243 AA; 27415 MW; 2FD377F574CD0A8A CRC64;
MNASQDTIYA QVSEHISDFQ FDSRVAGVFS DMIRRSVPGY TQIINTIGDF ADRFVKPNTQ
VYDLGCSLGA ATLSIRRQIQ GRDCRIVAVD NSESMVIRCQ ENLNAYVSDT EVELICGDIR
DIHIENASLV VLNFTLQFLP PEDRDALIAK IYQGLNPGGL LVLSEKIRFD DAPIQSVLEE
LHLDFKRANG YSELEISQKR SALENVMKPD TLSTHQQRLT HQGFSHFSTW FQCFNFASMV
AIK