ID Q1JXV1_DESA6 Unreviewed; 195 AA.
AC Q1JXV1;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=O-methyltransferase, family 3 {ECO:0000313|EMBL:EAT15042.1};
GN ORFNames=Dace_1119 {ECO:0000313|EMBL:EAT15042.1};
OS Desulfuromonas acetoxidans (strain DSM 684 / 11070).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=281689 {ECO:0000313|EMBL:EAT15042.1, ECO:0000313|Proteomes:UP000005695};
RN [1] {ECO:0000313|EMBL:EAT15042.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans DSM
RT 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT15042.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D.,
RA Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Desulfuromonas acetoxidans
RT DSM 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:8C9V}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH MG(2+).
RX PubMed=36942619; DOI=10.1002/cbic.202300076;
RA Sokolova N., Zhang L., Deravi S., Oerlemans R., Groves M.R., Haslinger K.;
RT "Structural Characterization and Extended Substrate Scope Analysis of Two
RT Mg2+ -Dependent O-Methyltransferases from Bacteria. .";
RL ChemBioChem 24:e202300076-e202300076(2023).
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:EAT15042.1}.
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DR EMBL; AAEW02000014; EAT15042.1; -; Genomic_DNA.
DR RefSeq; WP_006001606.1; NZ_AAEW02000014.1.
DR PDB; 8C9V; X-ray; 1.50 A; A=1-195.
DR AlphaFoldDB; Q1JXV1; -.
DR SMR; Q1JXV1; -.
DR OrthoDB; 9811000at2; -.
DR Proteomes; UP000005695; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR PANTHER; PTHR43167; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G01830)-RELATED; 1.
DR PANTHER; PTHR43167:SF1; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G01830)-RELATED; 1.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:8C9V}; Metal-binding {ECO:0007829|PDB:8C9V};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EAT15042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005695};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAT15042.1}.
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:8C9V"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:8C9V"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:8C9V"
SQ SEQUENCE 195 AA; 21548 MW; ED1D067F3EE0DBC0 CRC64;
MNKELHQLLC ELEEFGQAND EKTEDRAQRM LNITPDTGEF LAVLVRAMNA RRVLEIGTSN
GYSTLWLADA VSAIDGSVTT VEYAEQKYRL AQKNFSRTSL AHRIDAILGD AGTILGNADD
AVYDLIFLDS ERSQYPGWWP DLKRLLRPGG LLVVDNALSH GEQMAPFKAL VEADVEFTTC
VVPVGKGEFL ATRSA
//
