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P40363 (SFGH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-formylglutathione hydrolase

Short name=FGH
EC=3.1.2.12
Gene names
Ordered Locus Names:YJL068C
ORF Names:HRE299, J1102
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine hydrolase involved in the detoxification of formaldehyde. Ref.4

Catalytic activity

S-formylglutathione + H2O = glutathione + formate.

Subunit structure

Monomer. Ref.4

Subcellular location

Cytoplasm Ref.4.

Miscellaneous

Present with 1750 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the esterase D family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7. Ref.4

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Serine esterase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processformaldehyde catabolic process

Inferred from mutant phenotype Ref.4. Source: SGD

   Cellular_componentcytosol

Inferred from direct assay Ref.4. Source: SGD

   Molecular_functionS-formylglutathione hydrolase activity

Inferred from direct assay Ref.4. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299S-formylglutathione hydrolase
PRO_0000210342

Sites

Active site1611Charge relay system By similarity
Active site2411Charge relay system By similarity
Active site2761Charge relay system By similarity

Secondary structure

....................................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40363 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BFA5DC02729E9AEF

FASTA29933,934
        10         20         30         40         50         60 
MKVVKEFSVC GGRLIKLSHN SNSTKTSMNV NIYLPKHYYA QDFPRNKRIP TVFYLSGLTC 

        70         80         90        100        110        120 
TPDNASEKAF WQFQADKYGF AIVFPDTSPR GDEVANDPEG SWDFGQGAGF YLNATQEPYA 

       130        140        150        160        170        180 
QHYQMYDYIH KELPQTLDSH FNKNGDVKLD FLDNVAITGH SMGGYGAICG YLKGYSGKRY 

       190        200        210        220        230        240 
KSCSAFAPIV NPSNVPWGQK AFKGYLGEEK AQWEAYDPCL LIKNIRHVGD DRILIHVGDS 

       250        260        270        280        290 
DPFLEEHLKP ELLLEAVKAT SWQDYVEIKK VHGFDHSYYF VSTFVPEHAE FHARNLGLI 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces cerevisiae includes the mitochondrial ribosomal protein L8."
Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.
Yeast 11:57-60(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Purification and properties of an esterase from the yeast Saccharomyces cerevisiae and identification of the encoding gene."
Degrassi G., Uotila L., Klima R., Venturi V.
Appl. Environ. Microbiol. 65:3470-3472(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-7, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34288 Genomic DNA. Translation: CAA84054.1.
Z49343 Genomic DNA. Translation: CAA89359.1.
X88851 Genomic DNA. Translation: CAA61307.1.
BK006943 Genomic DNA. Translation: DAA08731.1.
PIRS50803.
RefSeqNP_012467.1. NM_001181501.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PV1X-ray2.30A/B/C/D1-299[»]
3C6BX-ray2.17A1-299[»]
4FLMX-ray2.41A/B1-299[»]
4FOLX-ray2.07A/B/C/D1-299[»]
ProteinModelPortalP40363.
SMRP40363. Positions 1-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33687. 62 interactions.
DIPDIP-4988N.
MINTMINT-540859.
STRING4932.YJL068C.

Proteomic databases

MaxQBP40363.
PaxDbP40363.
PeptideAtlasP40363.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL068C; YJL068C; YJL068C.
GeneID853377.
KEGGsce:YJL068C.

Organism-specific databases

CYGDYJL068c.
SGDS000003604. YJL068C.

Phylogenomic databases

eggNOGCOG0627.
GeneTreeENSGT00390000011864.
HOGENOMHOG000263929.
KOK01070.
OMARNREHYQ.
OrthoDBEOG73Z34V.

Gene expression databases

GenevestigatorP40363.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERPTHR10061. PTHR10061. 1 hit.
PfamPF00756. Esterase. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR02821. fghA_ester_D. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40363.
NextBio973828.
PROP40363.

Entry information

Entry nameSFGH_YEAST
AccessionPrimary (citable) accession number: P40363
Secondary accession number(s): D6VWB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references