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Entry version 129 (29 Sep 2021)
Sequence version 1 (01 Mar 2003)
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Protein

Serine hydroxymethyltransferase

Gene

SHMT

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the interconversion of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, a source of one-carbon units used by thymidylate synthase to convert dUMP to dTMP for DNA synthesis (PubMed:11071283, PubMed:19591883, PubMed:24914963).

Binds to its own mRNA and to the mRNA of bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS) in vitro; the physiological relevance of this interaction is not clear (PubMed:19591883).

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphateUniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Redox regulation; active in reducing conditions, inactive in oxidizing conditions. The reduction of the cysteine pairs allows the access binding of the tetrahydrofolate substrate to its binding site. This mechanism appears to be unique to Plasmodium species.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3.71 sec(-1) with L-serine and tetrahydrofolate as substrates (at 37 degrees Celsius) (PubMed:19591883). kcat is 9.4 min(-1) with L-serine and tetrahydrofolate as substrates (at 37 degrees Celsius) (PubMed:19591883).1 Publication
  1. KM=123 µM for L-serine1 Publication
  2. KM=700 µM for L-serine (at 37 degrees Celsius)1 Publication
  3. KM=86 µM for tetrahydrofolate (THF)1 Publication
  4. KM=3400 µM for tetrahydrofolate (THF) (at 37 degrees Celsius)1 Publication
  5. KM=13 µM for pyridoxal 5'-phosphate (at 37 degrees Celsius)1 Publication
  1. Vmax=139 pmol/min/µg enzyme towards L-serine (at 37 degrees Celsius)1 Publication
  2. Vmax=188.5 pmol/min/µg enzyme towards tetrahydrofolate (THF) (at 37 degrees Celsius)1 Publication
  3. Vmax=113 pmol/min/µg enzyme towards pyridoxal 5'-phosphate (at 37 degrees Celsius)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54Pyridoxal phosphate; shared with dimeric partnerCombined sources1 Publication1
Binding sitei236Pyridoxal phosphateCombined sources1 Publication1
Binding sitei272Pyridoxal phosphate; via amide nitrogen and shared with dimeric partnerCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processOne-carbon metabolism
LigandPyridoxal phosphate

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q8I566

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00193

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine hydroxymethyltransferase1 Publication (EC:2.1.2.13 Publications)
Alternative name(s):
PfSHMTc1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SHMT1 Publication
ORF Names:PF3D7_1235600Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPlasmodium falciparum (isolate 3D7)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri36329 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001450 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
PlasmoDB:PF3D7_1235600

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Apicoplast, Cytoplasm, Mitochondrion, Nucleus, Plastid

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi125C → P: Severe loss of catalytic activity characterized by a severe loss in substrate affinity. 1 Publication1
Mutagenesisi129H → A: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi292F → E: No effect on catalytic activity. 1 Publication1
Mutagenesisi364C → A or S: No effect on catalytic activity. Active in both reducing and non-reducing conditions. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004493771 – 442Serine hydroxymethyltransferaseAdd BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi125 ↔ 364Inhibitory under oxidizing conditionsCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei237N6-(pyridoxal phosphate)lysineUniRule annotationCombined sources1 Publication1

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8I566

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8I566

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during the parasite erythrocyte stages, namely in trophozoites and schizonts.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1442
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8I566

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni100 – 102Pyridoxal phosphate bindingCombined sources1 Publication3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SHMT family.Curated

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
SHPAGLI

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8I566

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00378, SHMT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00051, SHMT, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015424, PyrdxlP-dep_Trfase
IPR015421, PyrdxlP-dep_Trfase_major
IPR015422, PyrdxlP-dep_Trfase_small
IPR001085, Ser_HO-MeTrfase
IPR039429, SHMT-like_dom

The PANTHER Classification System

More...
PANTHERi
PTHR11680, PTHR11680, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00464, SHMT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000412, SHMT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383, SSF53383, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q8I566-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNNDPLQKY DKELFDLLEK EKNRQIETIN LIASENLTNT AVRECLGDRI
60 70 80 90 100
SNKYSEGYPH KRYYGGNDYV DKIEELCYKR ALEAFNVSEE EWGVNVQPLS
110 120 130 140 150
GSAANVQALY ALVGVKGKIM GMHLCSGGHL THGFFDEKKK VSITSDLFES
160 170 180 190 200
KLYKCNSEGY VDMESVRNLA LSFQPKVIIC GYTSYPRDID YKGFREICDE
210 220 230 240 250
VNAYLFADIS HISSFVACNL LNNPFTYADV VTTTTHKILR GPRSALIFFN
260 270 280 290 300
KKRNPGIDQK INSSVFPSFQ GGPHNNKIAA VACQLKEVNT PFFKEYTKQV
310 320 330 340 350
LLNSKALAEC LLKRNLDLVT NGTDNHLIVV DLRKYNITGS KLQETCNAIN
360 370 380 390 400
IALNKNTIPS DVDCVSPSGI RIGTPALTTR GCKEKDMEFI ADMLLKAILL
410 420 430 440
TDELQQKYGK KLVDFKKGLV NNPKIDELKK EVVQWAKNLP FA
Length:442
Mass (Da):49,780
Last modified:March 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i87E1C14AAFF0B8E7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
LN999947 Genomic DNA Translation: CZT99515.1

NCBI Reference Sequences

More...
RefSeqi
XP_001350750.1, XM_001350714.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
CZT99515; CZT99515; PF3D7_1235600

GeneDB pathogen genome database from Sanger Institute

More...
GeneDBi
PF3D7_1235600.1:pep

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
811396

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pfa:PF3D7_1235600

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LN999947 Genomic DNA Translation: CZT99515.1
RefSeqiXP_001350750.1, XM_001350714.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4O6ZX-ray2.98A/B/C/D1-442[»]
SMRiQ8I566
ModBaseiSearch...
PDBe-KBiSearch...

PTM databases

SwissPalmiQ8I566

Proteomic databases

PRIDEiQ8I566

Genome annotation databases

EnsemblProtistsiCZT99515; CZT99515; PF3D7_1235600
GeneDBiPF3D7_1235600.1:pep
GeneIDi811396
KEGGipfa:PF3D7_1235600

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_1235600

Phylogenomic databases

OMAiSHPAGLI
PhylomeDBiQ8I566

Enzyme and pathway databases

UniPathwayiUPA00193
SABIO-RKiQ8I566

Family and domain databases

CDDicd00378, SHMT, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
HAMAPiMF_00051, SHMT, 1 hit
InterProiView protein in InterPro
IPR015424, PyrdxlP-dep_Trfase
IPR015421, PyrdxlP-dep_Trfase_major
IPR015422, PyrdxlP-dep_Trfase_small
IPR001085, Ser_HO-MeTrfase
IPR039429, SHMT-like_dom
PANTHERiPTHR11680, PTHR11680, 1 hit
PfamiView protein in Pfam
PF00464, SHMT, 1 hit
PIRSFiPIRSF000412, SHMT, 1 hit
SUPFAMiSSF53383, SSF53383, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLYA_PLAF7
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8I566
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 22, 2020
Last sequence update: March 1, 2003
Last modified: September 29, 2021
This is version 129 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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