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Protein

S-formylglutathione hydrolase

Gene

SFGH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine hydrolase involved in the detoxification of formaldehyde.1 Publication

Catalytic activityi

S-formylglutathione + H2O = glutathione + formate.

Enzyme regulationi

Activity toward p-nitrophenyl acetate inhibited by N-ethylmaleimide, 10-(fluoroethoxyphosphinyl)-N-(biotinamidopentyl)decanamide (FP-biotin), iodoacetamide, CuCl2 and ZnSO4, but not by phenylmethylsulfonyl fluoride, EDTA, Mg2+, Mn2+, Ca2+ or paraoxon, an organo-phosphate inhibitor of serine hydrolases.1 Publication

Kineticsi

  1. KM=0.13 mM for S-formylglutathione
  2. KM=0.15 mM for S-acetylglutathione
  3. KM=1.02 mM for p-nitrophenyl acetate
  4. KM=0.57 mM for alpha-naphthyl acetate
  5. KM=0.54 mM for beta-naphthyl acetate
  6. KM=0.03 mM for fluorescein diacetate
  7. KM=0.12 mM for 4-methylumbelliferyl acetate
  1. Vmax=219 nmol/sec/mg enzyme for S-formylglutathione
  2. Vmax=311 nmol/sec/mg enzyme for S-acetylglutathione
  3. Vmax=185 nmol/sec/mg enzyme for p-nitrophenyl acetate
  4. Vmax=350 nmol/sec/mg enzyme for alpha-naphthyl acetate
  5. Vmax=22 nmol/sec/mg enzyme for beta-naphthyl acetate
  6. Vmax=3 nmol/sec/mg enzyme for fluorescein diacetate
  7. Vmax=714 nmol/sec/mg enzyme for 4-methylumbelliferyl acetate

pH dependencei

Optimum pH is 7.6-8 for carboxyesterase activity.

Temperature dependencei

Fully active up to 55 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Substrate
Binding sitei67 – 671Substrate
Active sitei152 – 1521Charge relay systemBy similarity
Active sitei229 – 2291Charge relay systemBy similarity
Active sitei262 – 2621Charge relay systemBy similarity

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • S-formylglutathione hydrolase activity Source: TAIR

GO - Biological processi

  • formaldehyde catabolic process Source: InterPro
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciARA:AT2G41530-MONOMER.
BRENDAi3.1.2.12. 399.
ReactomeiR-ATH-156590. Glutathione conjugation.

Protein family/group databases

ESTHERiarath-SFGH. A85-EsteraseD-FGH.

Names & Taxonomyi

Protein namesi
Recommended name:
S-formylglutathione hydrolase (EC:3.1.2.12)
Short name:
AtSFGH
Alternative name(s):
Esterase D
Gene namesi
Name:SFGH
Ordered Locus Names:At2g41530
ORF Names:T32G6.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G41530.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591C → S: Loss of catalysis regulation. 1 Publication
Mutagenesisi152 – 1521S → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 284283S-formylglutathione hydrolasePRO_0000248156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ8LAS8.
PRIDEiQ8LAS8.

PTM databases

iPTMnetiQ8LAS8.

Expressioni

Gene expression databases

GenevisibleiQ8LAS8. AT.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4088. 2 interactions.
IntActiQ8LAS8. 1 interaction.
MINTiMINT-8069064.
STRINGi3702.AT2G41530.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LAS8.
SMRiQ8LAS8. Positions 5-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the esterase D family.Curated

Phylogenomic databases

eggNOGiKOG3101. Eukaryota.
COG0627. LUCA.
HOGENOMiHOG000263929.
InParanoidiQ8LAS8.
KOiK01070.
OMAiHIKHHAK.
OrthoDBiEOG09360HPP.
PhylomeDBiQ8LAS8.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERiPTHR10061. PTHR10061. 1 hit.
PfamiPF00756. Esterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR02821. fghA_ester_D. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8LAS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGLSEIGS TKMFDGYNKR YKHFSETLGC SMTFSIYFPP SASSSHKSPV
60 70 80 90 100
LYWLSGLTCT DENFIIKSGA QRAASTHGIA LVAPDTSPRG LNVEGEADSY
110 120 130 140 150
DFGVGAGFYL NATQEKWKNW RMYDYVVKEL PKLLSENFSQ LDTTKASISG
160 170 180 190 200
HSMGGHGALT IYLRNLDKYK SVSAFAPITN PINCAWGQKA FTNYLGDNKA
210 220 230 240 250
AWEEYDATCL ISKYNNLSAT ILIDQGENDQ FYPDQLLPSK FEEACKKVNA
260 270 280
PLLLRLHPGY DHSYYFIATF IEDHISHHAQ ALEL
Length:284
Mass (Da):31,656
Last modified:September 5, 2006 - v2
Checksum:i44F69C31F14BAC29
GO

Sequence cautioni

The sequence AAM65175 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → N in AAM65175 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ347732 mRNA. Translation: CAC87877.1.
AC002510 Genomic DNA. Translation: AAB84335.1.
CP002685 Genomic DNA. Translation: AEC09995.1.
AY044322 mRNA. Translation: AAK73263.1.
AF446861 mRNA. Translation: AAL38594.1.
AF378875 mRNA. Translation: AAK55678.1.
AY087636 mRNA. Translation: AAM65175.1. Different initiation.
PIRiT00809.
RefSeqiNP_181684.1. NM_129716.3.
UniGeneiAt.12399.

Genome annotation databases

EnsemblPlantsiAT2G41530.1; AT2G41530.1; AT2G41530.
GeneIDi818751.
GrameneiAT2G41530.1; AT2G41530.1; AT2G41530.
KEGGiath:AT2G41530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ347732 mRNA. Translation: CAC87877.1.
AC002510 Genomic DNA. Translation: AAB84335.1.
CP002685 Genomic DNA. Translation: AEC09995.1.
AY044322 mRNA. Translation: AAK73263.1.
AF446861 mRNA. Translation: AAL38594.1.
AF378875 mRNA. Translation: AAK55678.1.
AY087636 mRNA. Translation: AAM65175.1. Different initiation.
PIRiT00809.
RefSeqiNP_181684.1. NM_129716.3.
UniGeneiAt.12399.

3D structure databases

ProteinModelPortaliQ8LAS8.
SMRiQ8LAS8. Positions 5-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4088. 2 interactions.
IntActiQ8LAS8. 1 interaction.
MINTiMINT-8069064.
STRINGi3702.AT2G41530.1.

Protein family/group databases

ESTHERiarath-SFGH. A85-EsteraseD-FGH.

PTM databases

iPTMnetiQ8LAS8.

Proteomic databases

PaxDbiQ8LAS8.
PRIDEiQ8LAS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G41530.1; AT2G41530.1; AT2G41530.
GeneIDi818751.
GrameneiAT2G41530.1; AT2G41530.1; AT2G41530.
KEGGiath:AT2G41530.

Organism-specific databases

TAIRiAT2G41530.

Phylogenomic databases

eggNOGiKOG3101. Eukaryota.
COG0627. LUCA.
HOGENOMiHOG000263929.
InParanoidiQ8LAS8.
KOiK01070.
OMAiHIKHHAK.
OrthoDBiEOG09360HPP.
PhylomeDBiQ8LAS8.

Enzyme and pathway databases

BioCyciARA:AT2G41530-MONOMER.
BRENDAi3.1.2.12. 399.
ReactomeiR-ATH-156590. Glutathione conjugation.

Miscellaneous databases

PROiQ8LAS8.

Gene expression databases

GenevisibleiQ8LAS8. AT.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERiPTHR10061. PTHR10061. 1 hit.
PfamiPF00756. Esterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR02821. fghA_ester_D. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSFGH_ARATH
AccessioniPrimary (citable) accession number: Q8LAS8
Secondary accession number(s): O22215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: September 7, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The conserved Cys-59, implicated in catalysis in cysteine hydrolases, lies in close proximity to the serine hydrolase triad, serving a gate-keeping function in regulating access to the active site via disulfide formation with glutathione.

Caution

Was originally classified as an esterase D due to its apparent insensitivity to serine hydrolase inhibitors.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.