GNMT_PIG
ID GNMT_PIG Reviewed; 295 AA.
AC Q29555; A5GFQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glycine N-methyltransferase;
DE EC=2.1.1.20 {ECO:0000269|PubMed:8281755};
GN Name=GNMT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Liver;
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).
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
CC (PubMed:8281755). Plays an important role in the regulation of methyl
CC group metabolism by regulating the ratio between S-adenosyl-L-
CC methionine and S-adenosyl-L-homocysteine (By similarity).
CC {ECO:0000250|UniProtKB:P13255, 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:8281755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19938;
CC Evidence={ECO:0000305|PubMed:8281755};
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 -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P13255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13255}.
CC -!- TISSUE SPECIFICITY: Abundant in liver.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Glycine N-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00932}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAN13168.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR956379; CAN13168.1; ALT_INIT; Genomic_DNA.
DR EMBL; D13308; BAA02568.1; -; mRNA.
DR RefSeq; NP_001103889.2; NM_001110419.2.
DR AlphaFoldDB; Q29555; -.
DR SMR; Q29555; -.
DR STRING; 9823.ENSSSCP00000001790; -.
DR PaxDb; Q29555; -.
DR PeptideAtlas; Q29555; -.
DR GeneID; 397444; -.
DR KEGG; ssc:397444; -.
DR CTD; 27232; -.
DR eggNOG; ENOG502QRN6; Eukaryota.
DR HOGENOM; CLU_069129_0_0_1; -.
DR InParanoid; Q29555; -.
DR OMA; YALKSRW; -.
DR OrthoDB; 1049906at2759; -.
DR TreeFam; TF324814; -.
DR BRENDA; 2.1.1.20; 6170.
DR SABIO-RK; Q29555; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000033214; Expressed in liver and 34 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR GO; GO:0017174; F:glycine N-methyltransferase activity; ISS:UniProtKB.
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; ISS: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 Cytoplasm; Folate-binding; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..295
FT /note="Glycine N-methyltransferase"
FT /id="PRO_0000087526"
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 139
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 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"
SQ SEQUENCE 295 AA; 32893 MW; DA626BF41DFE9F74 CRC64;
MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR
VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT
LDKDVPKSPM GGFDAVICQG NSFAHLPDCR GDQSEHRLAL KNITSMVRSG GLLVIDHRNY
DHILSTGCAP PGKNIYYKSD LIKDITTSVL TVNNKAHMVT LDYTVQVPGT GHRGSPGLSK
FRLSYYPHCL ASFTELLQTA FGGNGQHSVL GDFKPYKPGQ AYIPCYFIHV LRKTD
