ID W0R5V5_BIBTR Unreviewed; 240 AA.
AC W0R5V5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Carboxy-S-adenosyl-L-methionine synthase {ECO:0000256|HAMAP-Rule:MF_01589};
DE Short=Cx-SAM synthase {ECO:0000256|HAMAP-Rule:MF_01589};
DE EC=2.1.3.- {ECO:0000256|HAMAP-Rule:MF_01589};
GN Name=cmoA {ECO:0000256|HAMAP-Rule:MF_01589};
GN ORFNames=F544_12960 {ECO:0000313|EMBL:AHG86524.1};
OS Bibersteinia trehalosi USDA-ARS-USMARC-190.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Bibersteinia.
OX NCBI_TaxID=1263832 {ECO:0000313|EMBL:AHG86524.1, ECO:0000313|Proteomes:UP000019086};
RN [1] {ECO:0000313|EMBL:AHG86524.1, ECO:0000313|Proteomes:UP000019086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-190 {ECO:0000313|EMBL:AHG86524.1,
RC ECO:0000313|Proteomes:UP000019086};
RA Harhay G.P., McVey S., Clawson M.L., Bono J., Heaton M.P.,
RA Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT "Annotation of the Bibersteinia trehalosi USDA-ARS-USMARC-190 complete
RT genome.";
RL Submitted (DEC-2013) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01589};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01589}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cx-SAM synthase family. {ECO:0000256|HAMAP-Rule:MF_01589}.
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DR EMBL; CP006956; AHG86524.1; -; Genomic_DNA.
DR RefSeq; WP_015432673.1; NZ_CP006956.1.
DR AlphaFoldDB; W0R5V5; -.
DR KEGG; btra:F544_12960; -.
DR PATRIC; fig|1263832.3.peg.1287; -.
DR HOGENOM; CLU_078475_0_0_6; -.
DR Proteomes; UP000019086; Chromosome.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Methyltransferase {ECO:0000313|EMBL:AHG86524.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01589,
KW ECO:0000256|PIRSR:PIRSR006325-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01589}.
FT DOMAIN 58..156
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589,
FT ECO:0000256|PIRSR:PIRSR006325-1"
FT BINDING 62..64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589,
FT ECO:0000256|PIRSR:PIRSR006325-1"
FT BINDING 87..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589,
FT ECO:0000256|PIRSR:PIRSR006325-1"
FT BINDING 115..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589,
FT ECO:0000256|PIRSR:PIRSR006325-1"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589,
FT ECO:0000256|PIRSR:PIRSR006325-1"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589"
SQ SEQUENCE 240 AA; 27097 MW; 6642AB7F9BACC682 CRC64;
MKDTIFAAPI EKLGDFTFDE SVAEVFPDMI QRSVPGYSNI ITAIGMLAER FVTDNSQVYD
LGCSRGAGIL SVRRNVKAQN VKIIGIDNSE PMVERCRSHI NAYQSSIPVD IHLGDIRNVE
IENASMVILN FTLQFLPPHD RLALLKKIYQ GLKPNGVLVL SEKFTFANQA MNELLIDLHH
TFKRANGYSE LEVSQKRTAL ENVMRTDSID THKQRLQQAG FSQVELWFQC FNFGSMIAIK
//
