ID W5NKS3_LEPOC Unreviewed; 296 AA.
AC W5NKS3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycine N-methyltransferase {ECO:0000256|ARBA:ARBA00019972, ECO:0000256|PIRNR:PIRNR000385};
DE EC=2.1.1.20 {ECO:0000256|ARBA:ARBA00011999, ECO:0000256|PIRNR:PIRNR000385};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000021232.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000021232.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-
CC homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00033668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19938;
CC Evidence={ECO:0000256|ARBA:ARBA00033668};
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; AHAT01029867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NKS3; -.
DR STRING; 7918.ENSLOCP00000021232; -.
DR Ensembl; ENSLOCT00000021268.1; ENSLOCP00000021232.1; ENSLOCG00000017179.1.
DR eggNOG; ENOG502QRN6; Eukaryota.
DR GeneTree; ENSGT00390000006845; -.
DR HOGENOM; CLU_069129_0_0_1; -.
DR InParanoid; W5NKS3; -.
DR OMA; GKCQHSI; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000017179; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0017174; F:glycine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IBA:GO_Central.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IBA:GO_Central.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IBA:GO_Central.
DR GO; GO:1901052; P:sarcosine metabolic process; IBA:GO_Central.
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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16458; GLYCINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR16458:SF2; GLYCINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR PIRSF; PIRSF000385; Gly_N-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51600; SAM_GNMT; 1.
PE 3: Inferred from homology;
KW Folate-binding {ECO:0000256|ARBA:ARBA00022954};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR000385};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 60..203
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 32
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 118..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
SQ SEQUENCE 296 AA; 33477 MW; D3F846BA8A8DE637 CRC64;
VMVDSVYRTR SLGVAAVGLP DQYADGKAAK VWQLYIGDTR SRTDEYRSWL LSLLKKHGCQ
RVLDVACGTG VDSIMLVEEG FKVMSVDASD KMLKYALKAR WERRKEESFD QWVIEEANWL
SLPDDVEVPG NGFDAVICLG NSFAHLPDFK GDQSDQKLAL KNIASMVKPG GILIIDHRNY
DYILETGKAP QGKNTYYKSD LTQDITTSVL WVNSKPHMVT LDYTVQVPQP QGQQSTPELS
KFRLSYYPHC LDNFKQLLME AFGRKCEHSV FGDFMAYSPG QSHVPCYFIH VVRKTA
//
