ID A0A151UJ41_9GAMM Unreviewed; 247 AA.
AC A0A151UJ41;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BG74_08710 {ECO:0000313|EMBL:KYP95468.1};
OS Sodalis-like endosymbiont of Proechinophthirus fluctus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1462730 {ECO:0000313|EMBL:KYP95468.1, ECO:0000313|Proteomes:UP000217500};
RN [1] {ECO:0000313|EMBL:KYP95468.1, ECO:0000313|Proteomes:UP000217500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPI-1 {ECO:0000313|EMBL:KYP95468.1,
RC ECO:0000313|Proteomes:UP000217500};
RA Boyd B.M., Allen J.M., Koga R., Fukatsu T., Sweet A.D., Johnson K.P.,
RA Reed D.L.;
RT "Two associated bacteria (Sodalis and Rickettsia) associated with the seal
RT louse Proechinophthirus fluctus (Phthirapter: Anoplura).";
RL Submitted (JUN-2015) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01589}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYP95468.1}.
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DR EMBL; LECR01000090; KYP95468.1; -; Genomic_DNA.
DR RefSeq; WP_066598086.1; NZ_LECR01000090.1.
DR AlphaFoldDB; A0A151UJ41; -.
DR STRING; 1462730.BG74_08710; -.
DR PATRIC; fig|1462730.3.peg.1643; -.
DR Proteomes; UP000217500; Unassembled WGS sequence.
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:KYP95468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217500};
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 60..158
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT BINDING 39
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 89..90
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 117..118
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 132
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 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589"
SQ SEQUENCE 247 AA; 27772 MW; 9F146CB91AE4367E CRC64;
MNHRDDLFSA PIASLGDWTF DDRVAEVFPD MIQRSVPGYS NIISMIGMLA GRFARVGTQI
YDLGCALGAA TLVMRRTIHH TDCRIIAVDN SPAMIARCRR HIEAFRAEIP TEIVEGDIHT
VPIENASLVV LNFTLQFLEP EQRQTLLNRI YRGLNPGGAV VLSEKFSFQD RCIGSLLFDM
HHDFKRANGY SELEISQKRS MLENVMLTDT VEVHKQRLAA AGFGHAEVWF QCFNFGSLIA
IKQESGQ
//
