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Protein

Serine hydroxymethyltransferase, cytosolic

Gene

SHM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interconversion of serine and glycine.

Catalytic activityi

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.

Cofactori

Pathway:itetrahydrofolate interconversion

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

GO - Molecular functioni

  • glycine hydroxymethyltransferase activity Source: SGD
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • glycine metabolic process Source: InterPro
  • L-serine metabolic process Source: InterPro
  • one-carbon metabolic process Source: SGD
  • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YLR058C-MONOMER.
YEAST:YLR058C-MONOMER.
ReactomeiREACT_284316. Carnitine synthesis.
REACT_324954. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydroxymethyltransferase, cytosolic (EC:2.1.2.1)
Short name:
SHMT
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene namesi
Name:SHM2
Synonyms:SHMT2
Ordered Locus Names:YLR058C
ORF Names:L2156
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR058c.
EuPathDBiFungiDB:YLR058C.
SGDiS000004048. SHM2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Serine hydroxymethyltransferase, cytosolicPRO_0000113516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphothreonine1 Publication
Modified residuei26 – 261Phosphoserine2 Publications
Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei429 – 4291Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP37291.
PaxDbiP37291.
PeptideAtlasiP37291.
PRIDEiP37291.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi31333. 67 interactions.
DIPiDIP-2602N.
IntActiP37291. 16 interactions.
MINTiMINT-423439.

Structurei

3D structure databases

ProteinModelPortaliP37291.
SMRiP37291. Positions 4-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SHMT family.Curated

Phylogenomic databases

eggNOGiCOG0112.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
InParanoidiP37291.
KOiK00600.
OMAiCKSIQAD.
OrthoDBiEOG7PVWZT.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37291-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPYTLSDAHH KLITSHLVDT DPEVDSIIKD EIERQKHSID LIASENFTST
60 70 80 90 100
SVFDALGTPL SNKYSEGYPG ARYYGGNEHI DRMEILCQQR ALKAFHVTPD
110 120 130 140 150
KWGVNVQTLS GSPANLQVYQ AIMKPHERLM GLYLPDGGHL SHGYATENRK
160 170 180 190 200
ISAVSTYFES FPYRVNPETG IIDYDTLEKN AILYRPKVLV AGTSAYCRLI
210 220 230 240 250
DYKRMREIAD KCGAYLMVDM AHISGLIAAG VIPSPFEYAD IVTTTTHKSL
260 270 280 290 300
RGPRGAMIFF RRGVRSINPK TGKEVLYDLE NPINFSVFPG HQGGPHNHTI
310 320 330 340 350
AALATALKQA ATPEFKEYQT QVLKNAKALE SEFKNLGYRL VSNGTDSHMV
360 370 380 390 400
LVSLREKGVD GARVEYICEK INIALNKNSI PGDKSALVPG GVRIGAPAMT
410 420 430 440 450
TRGMGEEDFH RIVQYINKAV EFAQQVQQSL PKDACRLKDF KAKVDEGSDV
460
LNTWKKEIYD WAGEYPLAV
Length:469
Mass (Da):52,218
Last modified:October 1, 1996 - v2
Checksum:i4A79F79ED30A5965
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti429 – 4291S → K in AAA21023 (PubMed:8132653).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22529 Genomic DNA. Translation: AAA21023.1.
X94607 Genomic DNA. Translation: CAA64305.1.
Z73230 Genomic DNA. Translation: CAA97588.1.
BK006945 Genomic DNA. Translation: DAA09376.1.
PIRiS61632.
RefSeqiNP_013159.1. NM_001181945.1.

Genome annotation databases

EnsemblFungiiYLR058C; YLR058C; YLR058C.
GeneIDi850747.
KEGGisce:YLR058C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22529 Genomic DNA. Translation: AAA21023.1.
X94607 Genomic DNA. Translation: CAA64305.1.
Z73230 Genomic DNA. Translation: CAA97588.1.
BK006945 Genomic DNA. Translation: DAA09376.1.
PIRiS61632.
RefSeqiNP_013159.1. NM_001181945.1.

3D structure databases

ProteinModelPortaliP37291.
SMRiP37291. Positions 4-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31333. 67 interactions.
DIPiDIP-2602N.
IntActiP37291. 16 interactions.
MINTiMINT-423439.

Proteomic databases

MaxQBiP37291.
PaxDbiP37291.
PeptideAtlasiP37291.
PRIDEiP37291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR058C; YLR058C; YLR058C.
GeneIDi850747.
KEGGisce:YLR058C.

Organism-specific databases

CYGDiYLR058c.
EuPathDBiFungiDB:YLR058C.
SGDiS000004048. SHM2.

Phylogenomic databases

eggNOGiCOG0112.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
InParanoidiP37291.
KOiK00600.
OMAiCKSIQAD.
OrthoDBiEOG7PVWZT.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciMetaCyc:YLR058C-MONOMER.
YEAST:YLR058C-MONOMER.
ReactomeiREACT_284316. Carnitine synthesis.
REACT_324954. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi966873.
PROiP37291.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine."
    McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F.-R., Tang S., Bognar A.L.
    J. Biol. Chem. 269:9155-9165(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 201238 / W303-1B.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins."
    Norbeck J., Blomberg A.
    Yeast 13:1519-1534(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 151-161 AND 274-281.
    Strain: ATCC 44827 / SKQ2N.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-26 AND SER-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLYC_YEAST
AccessioniPrimary (citable) accession number: P37291
Secondary accession number(s): D6VY60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.
Present with 67600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.