SFGH_ARATH
ID SFGH_ARATH Reviewed; 284 AA.
AC Q8LAS8; O22215;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000303|PubMed:11888210};
DE Short=AtSFGH {ECO:0000303|PubMed:11888210};
DE EC=3.1.2.12 {ECO:0000305|PubMed:11888210};
DE AltName: Full=Esterase D;
GN Name=SFGH; OrderedLocusNames=At2g41530; ORFNames=T32G6.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=11888210; DOI=10.1006/abbi.2002.2772;
RA Kordic S., Cummins I., Edwards R.;
RT "Cloning and characterization of an S-formylglutathione hydrolase from
RT Arabidopsis thaliana.";
RL Arch. Biochem. Biophys. 399:232-238(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=14646092; DOI=10.1107/s0907444903020031;
RA McAuley K.E., Cummins I., Papiz M., Edwards R., Fordham-Skelton A.P.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of S-formylglutathione hydrolase from Arabidopsis thaliana: effects of
RT pressure and selenomethionine substitution on space-group changes.";
RL Acta Crystallogr. D 59:2272-2274(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, MUTAGENESIS OF CYS-59 AND
RP SER-152, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=16626737; DOI=10.1016/j.jmb.2006.03.048;
RA Cummins I., McAuley K., Fordham-Skelton A., Schwoerer R., Steel P.G.,
RA Davis B.G., Edwards R.;
RT "Unique regulation of the active site of the serine esterase S-
RT formylglutathione hydrolase.";
RL J. Mol. Biol. 359:422-432(2006).
CC -!- FUNCTION: Serine hydrolase which catalyzes the hydrolysis of S-
CC formylglutathione to glutathione and formic acid (Probable). Also
CC hydrolyzes S-acetylglutathione and a range of carboxyesters in vitro
CC (PubMed:11888210). Involved in the detoxification of formaldehyde
CC (PubMed:16626737). {ECO:0000269|PubMed:11888210,
CC ECO:0000269|PubMed:16626737, ECO:0000305|PubMed:11888210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-formylglutathione = formate + glutathione + H(+);
CC Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12;
CC Evidence={ECO:0000305|PubMed:11888210};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14962;
CC Evidence={ECO:0000305|PubMed:11888210};
CC -!- ACTIVITY REGULATION: Activity toward p-nitrophenyl acetate inhibited by
CC N-ethylmaleimide, 10-(fluoroethoxyphosphinyl)-N-
CC (biotinamidopentyl)decanamide (FP-biotin), iodoacetamide, CuCl(2) and
CC ZnSO(4), but not by phenylmethylsulfonyl fluoride, EDTA, Mg(2+),
CC Mn(2+), Ca(2+) or paraoxon, an organo-phosphate inhibitor of serine
CC hydrolases. {ECO:0000269|PubMed:16626737}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for S-formylglutathione {ECO:0000269|PubMed:11888210};
CC KM=0.15 mM for S-acetylglutathione {ECO:0000269|PubMed:11888210};
CC KM=1.02 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:11888210};
CC KM=0.57 mM for alpha-naphthyl acetate {ECO:0000269|PubMed:11888210};
CC KM=0.54 mM for beta-naphthyl acetate {ECO:0000269|PubMed:11888210};
CC KM=0.03 mM for fluorescein diacetate {ECO:0000269|PubMed:11888210};
CC KM=0.12 mM for 4-methylumbelliferyl acetate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=219 nmol/sec/mg enzyme with S-formylglutathione as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=311 nmol/sec/mg enzyme with S-acetylglutathione as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=185 nmol/sec/mg enzyme with p-nitrophenyl acetate as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=350 nmol/sec/mg enzyme with alpha-naphthyl acetate as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=22 nmol/sec/mg enzyme with beta-naphthyl acetate as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=3 nmol/sec/mg enzyme with fluorescein diacetate as substrate
CC {ECO:0000269|PubMed:11888210};
CC Vmax=714 nmol/sec/mg enzyme with 4-methylumbelliferyl acetate as
CC substrate {ECO:0000269|PubMed:11888210};
CC pH dependence:
CC Optimum pH is 7.6-8 for carboxyesterase activity.;
CC Temperature dependence:
CC Fully active up to 55 degrees Celsius.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16626737}.
CC -!- MISCELLANEOUS: The conserved Cys-59, implicated in catalysis in
CC cysteine hydrolases, lies in close proximity to the serine hydrolase
CC triad, serving a gate-keeping function in regulating access to the
CC active site via disulfide formation with glutathione.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
CC -!- CAUTION: Was originally classified as an esterase D due to its apparent
CC insensitivity to serine hydrolase inhibitors.
CC {ECO:0000305|PubMed:11888210}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ347732; CAC87877.1; -; mRNA.
DR EMBL; AC002510; AAB84335.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09995.1; -; Genomic_DNA.
DR EMBL; AY044322; AAK73263.1; -; mRNA.
DR EMBL; AF446861; AAL38594.1; -; mRNA.
DR EMBL; AF378875; AAK55678.1; -; mRNA.
DR EMBL; AY087636; AAM65175.1; ALT_INIT; mRNA.
DR PIR; T00809; T00809.
DR RefSeq; NP_181684.1; NM_129716.4.
DR AlphaFoldDB; Q8LAS8; -.
DR SMR; Q8LAS8; -.
DR BioGRID; 4088; 2.
DR IntAct; Q8LAS8; 1.
DR STRING; 3702.AT2G41530.1; -.
DR ESTHER; arath-SFGH; A85-EsteraseD-FGH.
DR iPTMnet; Q8LAS8; -.
DR PaxDb; Q8LAS8; -.
DR PRIDE; Q8LAS8; -.
DR ProteomicsDB; 232578; -.
DR EnsemblPlants; AT2G41530.1; AT2G41530.1; AT2G41530.
DR GeneID; 818751; -.
DR Gramene; AT2G41530.1; AT2G41530.1; AT2G41530.
DR KEGG; ath:AT2G41530; -.
DR Araport; AT2G41530; -.
DR TAIR; locus:2062729; AT2G41530.
DR eggNOG; KOG3101; Eukaryota.
DR HOGENOM; CLU_056472_0_1_1; -.
DR InParanoid; Q8LAS8; -.
DR OMA; TFMEDHL; -.
DR OrthoDB; 942551at2759; -.
DR PhylomeDB; Q8LAS8; -.
DR BioCyc; ARA:AT2G41530-MON; -.
DR BRENDA; 3.1.2.12; 399.
DR PRO; PR:Q8LAS8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LAS8; baseline and differential.
DR Genevisible; Q8LAS8; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IDA:TAIR.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Reference proteome; Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..284
FT /note="S-formylglutathione hydrolase"
FT /id="PRO_0000248156"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT BINDING 67
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 59
FT /note="C->S: Loss of catalysis regulation."
FT /evidence="ECO:0000269|PubMed:16626737"
FT MUTAGEN 152
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16626737"
FT CONFLICT 3
FT /note="S -> N (in Ref. 5; AAM65175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31656 MW; 44F69C31F14BAC29 CRC64;
MASGLSEIGS TKMFDGYNKR YKHFSETLGC SMTFSIYFPP SASSSHKSPV LYWLSGLTCT
DENFIIKSGA QRAASTHGIA LVAPDTSPRG LNVEGEADSY DFGVGAGFYL NATQEKWKNW
RMYDYVVKEL PKLLSENFSQ LDTTKASISG HSMGGHGALT IYLRNLDKYK SVSAFAPITN
PINCAWGQKA FTNYLGDNKA AWEEYDATCL ISKYNNLSAT ILIDQGENDQ FYPDQLLPSK
FEEACKKVNA PLLLRLHPGY DHSYYFIATF IEDHISHHAQ ALEL
