ID   A0A151X467_9HYME        Unreviewed;       291 AA.
AC   A0A151X467;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glycine N-methyltransferase {ECO:0000256|ARBA:ARBA00019972};
DE            EC=2.1.1.20 {ECO:0000256|ARBA:ARBA00011999};
GN   ORFNames=ALC60_05850 {ECO:0000313|EMBL:KYQ55225.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ55225.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ55225.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ55225.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ55225.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ982548; KYQ55225.1; -; Genomic_DNA.
DR   RefSeq; XP_018303840.1; XM_018448338.1.
DR   AlphaFoldDB; A0A151X467; -.
DR   STRING; 64791.A0A151X467; -.
DR   GeneID; 108722946; -.
DR   OrthoDB; 2902671at2759; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0017174; F:glycine 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; 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:UP000075809};
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..179
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
FT   BINDING         22
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         31
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000385-2"
FT   BINDING         117..118
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   291 AA;  33636 MW;  92C6F12C4C95D9DD CRC64;
     MVDSVFRTRS LGTPAEGVKD QYADGKAAKV WEVFIGDKNQ RTQNYRDFLV GLLRQKGCRR
     ILDVACGTGV DSVMLLEEGF EVVSVDASDK MLKYALKSRW NRRKEPAFDN WVIEEANWLT
     LSNDISHLIG EGFDAVICLG NSFAHMPDTF NDQREQRQAL VNFERCVKLG GLLLIDHRNY
     DYIIKTGQTP PKCIYYNSQH MTDIKTSVLF VSGKPKIVTM DYIVTLDEKN EDSEYISEFR
     LSYYPHRLTV FRDMLTEIFS HRAKHTIYGD FKPLNQIENP GFYIHVVQKQ H
//