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Database: UniProt
Entry: H2NSZ0_PONAB
LinkDB: H2NSZ0_PONAB
Original site: H2NSZ0_PONAB 
ID   H2NSZ0_PONAB            Unreviewed;       515 AA.
AC   H2NSZ0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   Name=SHMT1 {ECO:0000313|Ensembl:ENSPPYP00000009057.2};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000009057.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000009057.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPPYP00000009057.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {ECO:0000256|RuleBase:RU000585}.
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         Evidence={ECO:0000256|RuleBase:RU000585};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC       ECO:0000256|RuleBase:RU000585}.
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DR   AlphaFoldDB; H2NSZ0; -.
DR   Ensembl; ENSPPYT00000009425.2; ENSPPYP00000009057.2; ENSPPYG00000008051.3.
DR   GeneTree; ENSGT00390000002762; -.
DR   HOGENOM; CLU_022477_0_1_1; -.
DR   InParanoid; H2NSZ0; -.
DR   OMA; CQFANVQ; -.
DR   TreeFam; TF314667; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR   GO; GO:0070905; F:serine binding; IEA:Ensembl.
DR   GO; GO:1904482; P:cellular response to tetrahydrofolate; IEA:Ensembl.
DR   GO; GO:0046655; P:folic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0006565; P:L-serine catabolic process; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:Ensembl.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU000585};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          58..457
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         289
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   515 AA;  56699 MW;  55FA663501F3DF2B CRC64;
     MLPRLVLNSW EVIFSPQPLR VLGLQVQLRT SAMTMPVNGA HKDADLWSSH DKMLAQPLKD
     SDVEVYNIIK KESNRQRVGL ELIASENFAS RAVLEALGSC LNNKYSEGYP GQRYYGGTEF
     IDELETLCQK RALQAYKLDP QCWGVNVQPY SGSPANFAVY TALVEPHGRI MGLDLPDGGH
     LTHGFMTDKK KISATSIFFE SMPYKVNPDT GYINYDQLEE NARLFHPKLI IAGTSCYSRN
     LDYARLRKIA DENGAYLMAD MAHISGLVAA GVVPSPFEHC HVVTTTTHKT LRGCRAGMIF
     YRKGVQSVDP KTGKEILYNL ESLINSAVFP GLQGGPHNHA IAGVAVALKQ AMTLEFKVYQ
     HQVVANCRAL SEALTELGYK IVTGGSDNHL ILVDLRSKGT DGGRAEKVLE ACSIACNKNT
     CPGDRSALRP SGLRLGTPAL TSRGLLEKDF QKVAHFIHRG IELTLQIQSD TGVRATLKEF
     KERLAGDKYQ GAVQALREEV ESFASLFPLP GLPDF
//
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