ID   GNMT_HUMAN              Reviewed;         295 AA.
AC   Q14749; Q5T8W2; Q9NNZ1; Q9NS24;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Glycine N-methyltransferase {ECO:0000305};
DE            EC=2.1.1.20 {ECO:0000269|PubMed:14651980, ECO:0000269|PubMed:14739680, ECO:0000269|PubMed:17660255, ECO:0000269|PubMed:8281755};
GN   Name=GNMT {ECO:0000312|HGNC:HGNC:4415};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9495250;
RX   DOI=10.1002/(sici)1097-0215(19980302)75:5<787::aid-ijc20>3.0.co;2-2;
RA   Chen Y.-M.A., Shiu J.Y., Tzeng S.J., Shih L.S., Chen Y.J., Lui W.Y.,
RA   Chen P.H.;
RT   "Characterization of glycine-N-methyltransferase-gene expression in human
RT   hepatocellular carcinoma.";
RL   Int. J. Cancer 75:787-793(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=10843803; DOI=10.1006/geno.2000.6188;
RA   Chen Y.-M.A., Chen L.-Y., Wong F.H., Lee C.M., Chang T.J., Yang-Feng T.L.;
RT   "Genomic structure, expression, and chromosomal localization of the human
RT   glycine N-methyltransferase gene.";
RL   Genomics 66:43-47(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-295, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=8281755; DOI=10.1016/0305-0491(93)90137-t;
RA   Ogawa H., Gomi T., Fujioka M.;
RT   "Mammalian glycine N-methyltransferases. Comparative kinetic and structural
RT   properties of the enzymes from human, rat, rabbit and pig livers.";
RL   Comp. Biochem. Physiol. 106B:601-611(1993).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-294, AND SUBUNIT.
RX   PubMed=15340920; DOI=10.1002/prot.20209;
RA   Pakhomova S., Luka Z., Grohmann S., Wagner C., Newcomer M.E.;
RT   "Glycine N-methyltransferases: a comparison of the crystal structures and
RT   kinetic properties of recombinant human, mouse and rat enzymes.";
RL   Proteins 57:331-337(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-294, SUBUNIT, FUNCTION,
RP   CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT GNMT DEFICIENCY
RP   ASN-177.
RX   PubMed=17660255; DOI=10.1110/ps.072921507;
RA   Luka Z., Pakhomova S., Luka Y., Newcomer M.E., Wagner C.;
RT   "Destabilization of human glycine N-methyltransferase by H176N mutation.";
RL   Protein Sci. 16:1957-1964(2007).
RN   [10]
RP   VARIANTS GNMT DEFICIENCY PRO-50 AND ASN-177.
RX   PubMed=11810299; DOI=10.1007/s00439-001-0648-4;
RA   Luka Z., Cerone R., Phillips J.A. III, Mudd S.H., Wagner C.;
RT   "Mutations in human glycine N-methyltransferase give insights into its role
RT   in methionine metabolism.";
RL   Hum. Genet. 110:68-74(2002).
RN   [11]
RP   CHARACTERIZATION OF VARIANTS GNMT DEFICIENCY PRO-50; SER-141 AND ASN-177,
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14651980; DOI=10.1016/j.bbrc.2003.11.037;
RA   Luka Z., Wagner C.;
RT   "Effect of naturally occurring mutations in human glycine N-
RT   methyltransferase on activity and conformation.";
RL   Biochem. Biophys. Res. Commun. 312:1067-1072(2003).
RN   [12]
RP   VARIANT GNMT DEFICIENCY SER-141, CHARACTERIZATION OF VARIANT GNMT
RP   DEFICIENCY SER-141, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14739680; DOI=10.1023/b:boli.0000009978.17777.33;
RA   Augoustides-Savvopoulou P., Luka Z., Karyda S., Stabler S.P., Allen R.H.,
RA   Patsiaoura K., Wagner C., Mudd S.H.;
RT   "Glycine N-methyltransferase deficiency: a new patient with a novel
RT   mutation.";
RL   J. Inherit. Metab. Dis. 26:745-759(2003).
CC   -!- FUNCTION: Catalyzes the methylation of glycine by using S-
CC       adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with
CC       the concomitant production of S-adenosylhomocysteine (AdoHcy), a
CC       reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an
CC       important role in the regulation of methyl group metabolism by
CC       regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-
CC       homocysteine. {ECO:0000269|PubMed:14651980,
CC       ECO:0000269|PubMed:14739680, ECO:0000269|PubMed:17660255,
CC       ECO:0000269|PubMed:8281755}.
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:0000269|PubMed:14651980, ECO:0000269|PubMed:14739680,
CC         ECO:0000269|PubMed:17660255, ECO:0000269|PubMed:8281755};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19938;
CC         Evidence={ECO:0000305|PubMed:14651980};
CC   -!- ACTIVITY REGULATION: Inhibited by 5-methyltetrahydrofolate
CC       monoglutamate and by 5-methyltetrahydrofolate pentaglutamate,
CC       inhibition is much more effective by the pentaglutamate form than by
CC       the monoglutamate form. Two molecules of 5-methyltetrahydrofolate are
CC       bound per tetramer. The binding sites are localized between subunits.
CC       Inhibitor binding may preclude movements of the polypeptide chain that
CC       are necessary for enzyme activity. {ECO:0000250|UniProtKB:P13255}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=281 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:14651980};
CC         KM=12.2 uM for glycine {ECO:0000269|PubMed:14651980};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15340920,
CC       ECO:0000269|PubMed:17660255}.
CC   -!- INTERACTION:
CC       Q14749; P49407: ARRB1; NbExp=12; IntAct=EBI-744239, EBI-743313;
CC       Q14749; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-744239, EBI-11974185;
CC       Q14749; P24311: COX7B; NbExp=3; IntAct=EBI-744239, EBI-2684371;
CC       Q14749; O60931-2: CTNS; NbExp=3; IntAct=EBI-744239, EBI-19888994;
CC       Q14749; Q14331: FRG1; NbExp=3; IntAct=EBI-744239, EBI-2515248;
CC       Q14749; Q9UN88: GABRQ; NbExp=3; IntAct=EBI-744239, EBI-12820585;
CC       Q14749; Q13066: GAGE2C; NbExp=3; IntAct=EBI-744239, EBI-12329121;
CC       Q14749; A0A0S2Z5F2: GNMT; NbExp=3; IntAct=EBI-744239, EBI-16440982;
CC       Q14749; Q14749: GNMT; NbExp=6; IntAct=EBI-744239, EBI-744239;
CC       Q14749; P00492: HPRT1; NbExp=3; IntAct=EBI-744239, EBI-748210;
CC       Q14749; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-744239, EBI-741158;
CC       Q14749; O75643: SNRNP200; NbExp=3; IntAct=EBI-744239, EBI-1045395;
CC       Q14749; P31213: SRD5A2; NbExp=3; IntAct=EBI-744239, EBI-13130472;
CC       Q14749; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-744239, EBI-17716262;
CC       Q14749; Q9Y3M9: ZNF337; NbExp=3; IntAct=EBI-744239, EBI-714987;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13255}.
CC   -!- TISSUE SPECIFICITY: Expressed only in liver, pancreas, and prostate.
CC       {ECO:0000269|PubMed:9495250}.
CC   -!- DISEASE: Glycine N-methyltransferase deficiency (GNMT deficiency)
CC       [MIM:606664]: The only clinical abnormalities in patients with this
CC       deficiency are mild hepatomegaly and chronic elevation of serum
CC       transaminases. {ECO:0000269|PubMed:11810299,
CC       ECO:0000269|PubMed:14739680}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Glycine N-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00932}.
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DR   EMBL; AF101477; AAF78290.1; -; mRNA.
DR   EMBL; AF101475; AAF78289.1; -; Genomic_DNA.
DR   EMBL; AL158815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04124.1; -; Genomic_DNA.
DR   EMBL; BC032627; AAH32627.1; -; mRNA.
DR   EMBL; X62250; CAA44164.1; -; mRNA.
DR   CCDS; CCDS4876.1; -.
DR   PIR; S42627; S42627.
DR   RefSeq; NP_001305794.1; NM_001318865.1.
DR   RefSeq; NP_061833.1; NM_018960.5.
DR   PDB; 1R74; X-ray; 2.55 A; A/B=2-295.
DR   PDB; 2AZT; X-ray; 2.70 A; A/B=1-295.
DR   PDBsum; 1R74; -.
DR   PDBsum; 2AZT; -.
DR   AlphaFoldDB; Q14749; -.
DR   SMR; Q14749; -.
DR   BioGRID; 118081; 40.
DR   IntAct; Q14749; 26.
DR   MINT; Q14749; -.
DR   STRING; 9606.ENSP00000361894; -.
DR   BindingDB; Q14749; -.
DR   ChEMBL; CHEMBL4523295; -.
DR   DrugBank; DB00118; Ademetionine.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR   iPTMnet; Q14749; -.
DR   PhosphoSitePlus; Q14749; -.
DR   BioMuta; GNMT; -.
DR   DMDM; 12644416; -.
DR   MassIVE; Q14749; -.
DR   PaxDb; 9606-ENSP00000361894; -.
DR   PeptideAtlas; Q14749; -.
DR   ProteomicsDB; 60155; -.
DR   Antibodypedia; 16133; 410 antibodies from 30 providers.
DR   DNASU; 27232; -.
DR   Ensembl; ENST00000372808.4; ENSP00000361894.3; ENSG00000124713.6.
DR   GeneID; 27232; -.
DR   KEGG; hsa:27232; -.
DR   MANE-Select; ENST00000372808.4; ENSP00000361894.3; NM_018960.6; NP_061833.1.
DR   AGR; HGNC:4415; -.
DR   CTD; 27232; -.
DR   DisGeNET; 27232; -.
DR   GeneCards; GNMT; -.
DR   HGNC; HGNC:4415; GNMT.
DR   HPA; ENSG00000124713; Group enriched (liver, pancreas).
DR   MalaCards; GNMT; -.
DR   MIM; 606628; gene.
DR   MIM; 606664; phenotype.
DR   neXtProt; NX_Q14749; -.
DR   OpenTargets; ENSG00000124713; -.
DR   Orphanet; 289891; Hypermethioninemia due to glycine N-methyltransferase deficiency.
DR   PharmGKB; PA28794; -.
DR   VEuPathDB; HostDB:ENSG00000124713; -.
DR   eggNOG; ENOG502QRN6; Eukaryota.
DR   GeneTree; ENSGT00390000006845; -.
DR   HOGENOM; CLU_069129_0_0_1; -.
DR   InParanoid; Q14749; -.
DR   OMA; GKCQHSI; -.
DR   OrthoDB; 2902671at2759; -.
DR   PhylomeDB; Q14749; -.
DR   TreeFam; TF324814; -.
DR   BRENDA; 2.1.1.20; 2681.
DR   PathwayCommons; Q14749; -.
DR   Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR   Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR   SABIO-RK; Q14749; -.
DR   SignaLink; Q14749; -.
DR   SIGNOR; Q14749; -.
DR   BioGRID-ORCS; 27232; 13 hits in 1156 CRISPR screens.
DR   EvolutionaryTrace; Q14749; -.
DR   GeneWiki; GNMT; -.
DR   GenomeRNAi; 27232; -.
DR   Pharos; Q14749; Tchem.
DR   PRO; PR:Q14749; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q14749; Protein.
DR   Bgee; ENSG00000124713; Expressed in body of pancreas and 94 other cell types or tissues.
DR   ExpressionAtlas; Q14749; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR   GO; GO:0017174; F:glycine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IBA:GO_Central.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:Ensembl.
DR   GO; GO:0006555; P:methionine metabolic process; IEA:Ensembl.
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; IPI:UniProtKB.
DR   GO; GO:0036211; P:protein modification process; NAS:UniProtKB.
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; IDA:UniProtKB.
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; 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; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51600; SAM_GNMT; 1.
DR   Genevisible; Q14749; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Disease variant; Folate-binding;
KW   Methyltransferase; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   CHAIN           2..295
FT                   /note="Glycine N-methyltransferase"
FT                   /id="PRO_0000087524"
FT   BINDING         4
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         6
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         6
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         22
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         31
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         86..88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         139..142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         217
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         223
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         242
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   BINDING         242
FT                   /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:18608"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between tetrameric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   MOD_RES         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P13255"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   MOD_RES         34
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   MOD_RES         46
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   MOD_RES         193
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   MOD_RES         198
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   MOD_RES         203
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT   VARIANT         50
FT                   /note="L -> P (in GNMT deficiency; 10% wild-type glycine
FT                   N-methyltransferase activity; dbSNP:rs121907888)"
FT                   /evidence="ECO:0000269|PubMed:11810299,
FT                   ECO:0000269|PubMed:14651980"
FT                   /id="VAR_012766"
FT   VARIANT         141
FT                   /note="N -> S (in GNMT deficiency; 0.5% wild-type glycine
FT                   N-methyltransferase activity; dbSNP:rs864321678)"
FT                   /evidence="ECO:0000269|PubMed:14651980,
FT                   ECO:0000269|PubMed:14739680"
FT                   /id="VAR_019840"
FT   VARIANT         177
FT                   /note="H -> N (in GNMT deficiency; 75% wild-type glycine
FT                   N-methyltransferase activity, decreases stability of the
FT                   tetramer; dbSNP:rs121907889)"
FT                   /evidence="ECO:0000269|PubMed:11810299,
FT                   ECO:0000269|PubMed:14651980, ECO:0000269|PubMed:17660255"
FT                   /id="VAR_012767"
FT   CONFLICT        119
FT                   /note="Missing (in Ref. 6; CAA44164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129..130
FT                   /note="AE -> PK (in Ref. 2; AAF78289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="I -> S (in Ref. 6; CAA44164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256..260
FT                   /note="LLQAA -> SPSS (in Ref. 6; CAA44164)"
FT                   /evidence="ECO:0000305"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           43..55
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           89..101
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           106..109
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           154..165
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          167..178
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           180..186
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          215..225
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          239..245
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   HELIX           250..260
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          265..271
FT                   /evidence="ECO:0007829|PDB:1R74"
FT   STRAND          285..293
FT                   /evidence="ECO:0007829|PDB:1R74"
SQ   SEQUENCE   295 AA;  32742 MW;  34F4546136FD27ED CRC64;
     MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR
     VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT
     LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY
     DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK
     FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD
//