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Database: UniProt
Entry: W8KG30_9GAMM
LinkDB: W8KG30_9GAMM
Original site: W8KG30_9GAMM 
ID   W8KG30_9GAMM            Unreviewed;       269 AA.
AC   W8KG30;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:AHK78724.1};
GN   ORFNames=M911_05560 {ECO:0000313|EMBL:AHK78724.1};
OS   Ectothiorhodospira haloalkaliphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK78724.1, ECO:0000313|Proteomes:UP000019442};
RN   [1] {ECO:0000313|EMBL:AHK78724.1, ECO:0000313|Proteomes:UP000019442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|EMBL:AHK78724.1,
RC   ECO:0000313|Proteomes:UP000019442};
RX   PubMed=25057327; DOI=10.7150/jgen.9123;
RA   Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT   "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT   Sulfur Bacterium Halorhodospira halochloris.";
RL   J Genomics 2:118-120(2014).
RN   [2] {ECO:0000313|Proteomes:UP000019442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA   Singh K.S.;
RT   "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT   halochloris.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Glycine N-methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR000385}.
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DR   EMBL; CP007268; AHK78724.1; -; Genomic_DNA.
DR   RefSeq; WP_025281113.1; NZ_JAJNQR010000007.1.
DR   AlphaFoldDB; W8KG30; -.
DR   KEGG; hhc:M911_05560; -.
DR   PATRIC; fig|1354791.3.peg.1548; -.
DR   HOGENOM; CLU_069129_0_0_6; -.
DR   OrthoDB; 9772751at2; -.
DR   Proteomes; UP000019442; Chromosome.
DR   GO; GO:0017174; F:glycine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.46.10; Glycine N-methyltransferase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR16458; GLYCINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR16458:SF2; GLYCINE N-METHYLTRANSFERASE; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   PIRSF; PIRSF000385; Gly_N-mtase; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51600; SAM_GNMT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000385};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019442};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR000385};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000385}.
FT   DOMAIN          64..161
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         115..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
SQ   SEQUENCE   269 AA;  31355 MW;  92C37929553ED221 CRC64;
     MSNTMTDQDF GEKPVERRDT DNYVKEYTES FVDKWDDLID WDSRAKSEGD FFIQELKKRG
     AKRVLDVATG TGFHSVRLLE AGFDVVSVDG APEMLVKAFE NGRKRGHILR TTQADWRELN
     RDIYGRYDAV VCLGNSFTHL FNENDRRKAL AEFYAALNHD GVLILDQRNY DAILDHGYSS
     AHTFYYCGDN VSVYPEHVDD GLARFRYAFP DKSVFHLNMF PLRKPYVRRL MREVGFQNIE
     TYGDFKETYH DTEPDFFIHV ASKKYTGKE
//
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