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Database: UniProt
Entry: K9YF78_HALP7
LinkDB: K9YF78_HALP7
Original site: K9YF78_HALP7 
ID   K9YF78_HALP7            Unreviewed;       265 AA.
AC   K9YF78;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Glycine/sarcosine N-methyltransferase {ECO:0000313|EMBL:AFZ45621.1};
DE            EC=2.1.1.156 {ECO:0000313|EMBL:AFZ45621.1};
GN   OrderedLocusNames=PCC7418_3510 {ECO:0000313|EMBL:AFZ45621.1};
OS   Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX   NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45621.1, ECO:0000313|Proteomes:UP000010481};
RN   [1] {ECO:0000313|Proteomes:UP000010481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003945; AFZ45621.1; -; Genomic_DNA.
DR   RefSeq; WP_015227493.1; NC_019779.1.
DR   AlphaFoldDB; K9YF78; -.
DR   SMR; K9YF78; -.
DR   STRING; 65093.PCC7418_3510; -.
DR   KEGG; hao:PCC7418_3510; -.
DR   PATRIC; fig|65093.3.peg.3710; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_069129_0_0_3; -.
DR   OrthoDB; 9791837at2; -.
DR   Proteomes; UP000010481; Chromosome.
DR   GO; GO:0017174; F:glycine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0052730; F:sarcosine N-methyltransferase activity; IEA:UniProtKB-EC.
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:UP000010481};
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          65..162
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   BINDING         28
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         116..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
SQ   SEQUENCE   265 AA;  31213 MW;  DD65C73F70E44536 CRC64;
     MAIKEKQVQD YGENPIEVRD SDHYQNEYIE GFVEKWDELI NWHARSSSEG EFFIKTLKEH
     GAKRVLDAAT GTGFHSIRLI EAGFDVASVD GSVEMLVKAF ENATRKDQIL RTVHSDWRQV
     TRHIQERFDA VICLGNSFTH LFSEEDRRKT LAEFYSVLKH DGILILDQRN YDLILDEGFK
     SKHTYYYCGD NVKAEPEYVD DGLARFRYEF PDQSVYHLNM FPLRKDYVRR LLHEVGFQDI
     TTYGDFQETY HQDDPDFYIH VAKKD
//
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