GLYC_CAEEL
ID GLYC_CAEEL Reviewed; 507 AA.
AC P50432; Q95QX8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=Glycosylation-related protein 1;
DE AltName: Full=Maternal effect lethal protein 32;
DE AltName: Full=Serine methylase;
GN Name=mel-32; Synonyms=gly-1; ORFNames=C05D11.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP MUTAGENESIS OF ALA-86; ARG-107; ARG-125; ALA-126; ALA-149; GLY-166;
RP LEU-169; GLY-172; GLY-227; SER-274; HIS-282; ALA-291; GLY-336; GLY-395 AND
RP GLY-429.
RX PubMed=9497323; DOI=10.1074/jbc.273.11.6066;
RA Vatcher G.P., Thacker C.M., Kaletta T., Schnabel H., Schnabel R.,
RA Baillie D.L.;
RT "Serine hydroxymethyltransferase is maternally essential in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 273:6066-6073(1998).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P50432-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P50432-2; Sequence=VSP_006097;
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; FO080365; CCD63201.1; -; Genomic_DNA.
DR EMBL; FO080365; CCD63202.1; -; Genomic_DNA.
DR PIR; B88483; B88483.
DR RefSeq; NP_741197.1; NM_171169.4. [P50432-1]
DR RefSeq; NP_741198.1; NM_171170.4.
DR AlphaFoldDB; P50432; -.
DR SMR; P50432; -.
DR BioGRID; 41133; 19.
DR DIP; DIP-26240N; -.
DR IntAct; P50432; 2.
DR MINT; P50432; -.
DR STRING; 6239.C05D11.11b.1; -.
DR iPTMnet; P50432; -.
DR EPD; P50432; -.
DR PaxDb; P50432; -.
DR PeptideAtlas; P50432; -.
DR EnsemblMetazoa; C05D11.11a.1; C05D11.11a.1; WBGene00003214. [P50432-2]
DR EnsemblMetazoa; C05D11.11a.2; C05D11.11a.2; WBGene00003214. [P50432-2]
DR EnsemblMetazoa; C05D11.11a.3; C05D11.11a.3; WBGene00003214. [P50432-2]
DR EnsemblMetazoa; C05D11.11b.1; C05D11.11b.1; WBGene00003214. [P50432-1]
DR GeneID; 175915; -.
DR KEGG; cel:CELE_C05D11.11; -.
DR UCSC; F44F4.6; c. elegans. [P50432-1]
DR CTD; 175915; -.
DR WormBase; C05D11.11a; CE01130; WBGene00003214; mel-32. [P50432-2]
DR WormBase; C05D11.11b; CE29661; WBGene00003214; mel-32. [P50432-1]
DR eggNOG; KOG2467; Eukaryota.
DR GeneTree; ENSGT00390000002762; -.
DR InParanoid; P50432; -.
DR OMA; SHPAGLI; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; P50432; -.
DR Reactome; R-CEL-196757; Metabolism of folate and pterines.
DR Reactome; R-CEL-71262; Carnitine synthesis.
DR UniPathway; UPA00193; -.
DR PRO; PR:P50432; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003214; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
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:0009113; P:purine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0009069; P:serine family amino acid metabolic process; TAS:UniProtKB.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; One-carbon metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..507
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113508"
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_006097"
FT MUTAGEN 86
FT /note="A->V: In t1473; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype; when
FT associated with F-169."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 107
FT /note="R->Q: In t1597; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 125
FT /note="R->K: In t1555; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 126
FT /note="A->V: In t1666; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 149
FT /note="A->V: In s2518; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 166
FT /note="G->D: In t1679; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 169
FT /note="L->F: In t1473; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype; when
FT associated with V-86."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 172
FT /note="G->E: In t1665; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 227
FT /note="G->E: In t1552; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 274
FT /note="S->F: In t1520; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 282
FT /note="H->Y: In t1607; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 291
FT /note="A->T: In t1616; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 336
FT /note="G->E: In t1456; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 395
FT /note="G->R: In t1576; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
FT MUTAGEN 429
FT /note="G->E: In t1632; causes recessive maternal effect
FT lethal (Mel) phenotype where homozygotes are viable but
FT offspring display an embryonic lethal phenotype."
FT /evidence="ECO:0000269|PubMed:9497323"
SQ SEQUENCE 507 AA; 55765 MW; 693B380E77BB07D8 CRC64;
MFARIVSRRA ATGLFAGASS QCKMADRQVH TPLAKVQRHK YTNNENILVD HVEKVDPEVF
DIMKNEKKRQ RRGLELIASE NFTSKAVMDA LGSAMCNKYS EGYPGARYYG GNEFIDQMEL
LCQKRALEVF GLDPAKWGVN VQPLSGSPAN FAVYTAIVGS NGRIMGLDLP DGGHLTHGFF
TPARKVSATS EFFQSLPYKV DPTTGLIDYD KLEQNAMLFR PKAIIAGVSC YARHLDYERF
RKIATKAGAY LMSDMAHISG LVAAGLIPSP FEYSDVVTTT THKSLRGPRG ALIFYRKGVR
STNAKGVDTL YDLEEKINSA VFPGLQGGPH NHTIAGIAVA LRQCLSEDFV QYGEQVLKNA
KTLAERMKKH GYALATGGTD NHLLLVDLRP IGVEGARAEH VLDLAHIACN KNTCPGDVSA
LRPGGIRLGT PALTSRGFQE QDFEKVGDFI HEGVQIAKKY NAEAGKTLKD FKSFTETNEP
FKKDVADLAK RVEEFSTKFE IPGNETF
