GNMT_HUMAN
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 03-AUG-2022, entry version 193.
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 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; Q14749; -.
DR PeptideAtlas; Q14749; -.
DR PRIDE; Q14749; -.
DR ProteomicsDB; 60155; -.
DR Antibodypedia; 16133; 352 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 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; YALKSRW; -.
DR OrthoDB; 1049906at2759; -.
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 1072 CRISPR screens.
DR EvolutionaryTrace; Q14749; -.
DR GeneWiki; GNMT; -.
DR GenomeRNAi; 27232; -.
DR Pharos; Q14749; Tbio.
DR PRO; PR:Q14749; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14749; protein.
DR Bgee; ENSG00000124713; Expressed in body of pancreas and 94 other tissues.
DR ExpressionAtlas; Q14749; baseline and differential.
DR Genevisible; Q14749; HS.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16458; PTHR16458; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF000385; Gly_N-mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51600; SAM_GNMT; 1.
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 N-
FT 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 N-
FT 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
