ID E2C8H4_HARSA Unreviewed; 292 AA.
AC E2C8H4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Glycine N-methyltransferase {ECO:0000256|ARBA:ARBA00019972};
DE EC=2.1.1.20 {ECO:0000256|ARBA:ARBA00011999};
GN ORFNames=EAI_09704 {ECO:0000313|EMBL:EFN75704.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN75704.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN75704.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL453666; EFN75704.1; -; Genomic_DNA.
DR RefSeq; XP_011152511.1; XM_011154209.1.
DR AlphaFoldDB; E2C8H4; -.
DR STRING; 610380.E2C8H4; -.
DR EnsemblMetazoa; XM_011154209.2; XP_011152511.1; LOC105191076.
DR GeneID; 105191076; -.
DR KEGG; hst:105191076; -.
DR InParanoid; E2C8H4; -.
DR OMA; GKCQHSI; -.
DR OrthoDB; 2902671at2759; -.
DR PhylomeDB; E2C8H4; -.
DR Proteomes; UP000008237; 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:UP000008237};
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 59..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 292 AA; 33556 MW; 2244B810EB438504 CRC64;
MVDSVFRTRS LGTPAEGVKD QYADGKAAKV WEVFIGDKKL RTQNYRDFLV GLLRQKKCRR
ILDVACGTGV DSIMLLEEGF EVVSVDASDK MLKYALKSRW DRRKEPAFDK WVIEEANWLT
LSNDISHLIG EGFDAVICLG NSFAHMPDSF GDQREQRLAF SNFERCVKPG GLLLIDHRNY
DYIIRTGQTP SKCIYYNSQH MTDIKTSVLY VSGKPTIVTL DYMISLDNEN PDNPESISEF
RLSYYPHRLT VFRDMLTEVF GHGAKHTIYG DFKPLNQIED PGFYIHVLEK QR
//
