ID J0IWP9_HELPX Unreviewed; 247 AA.
AC J0IWP9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ECO:0000313|EMBL:EJB30065.1};
GN ORFNames=HPNQ4200_0382 {ECO:0000313|EMBL:EJB30065.1};
OS Helicobacter pylori NQ4200.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992024 {ECO:0000313|EMBL:EJB30065.1, ECO:0000313|Proteomes:UP000003358};
RN [1] {ECO:0000313|EMBL:EJB30065.1, ECO:0000313|Proteomes:UP000003358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NQ4200 {ECO:0000313|EMBL:EJB30065.1,
RC ECO:0000313|Proteomes:UP000003358};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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 -!- 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:EJB30065.1}.
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DR EMBL; AKNS01000003; EJB30065.1; -; Genomic_DNA.
DR RefSeq; WP_000655589.1; NZ_AKNS01000003.1.
DR AlphaFoldDB; J0IWP9; -.
DR PATRIC; fig|992024.3.peg.365; -.
DR Proteomes; UP000003358; 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:EJB30065.1};
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 68..162
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT BINDING 35
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 72..74
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 96..97
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 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01589"
SQ SEQUENCE 247 AA; 28947 MW; 9D759006E80A0390 CRC64;
MKDTLFNKSL NKRFCFDEKV AHVFDDMLER SIPYYHEMLN LGAYFIAQNL KENLYPKPLP
KSLPKPLIYD LGCSTGNFFI ALNQQIQQDI ELIGIDNSMP MLKKAQEKLK DFNNVRFECM
DFLEIEFREA SAFSLLFVLQ FVRPMQREVL LKKIYNSLAL NGVLLVGEKT MSEDRILDKQ
MIELYYLYKQ NQGYSHNEIA FKREALENVL VPYSLKENVA LLESVGFKHV EALFKWVNFT
LLVARKT
//
