ETHE1_ARATH
ID ETHE1_ARATH Reviewed; 294 AA.
AC Q9C8L4; Q93VR2; Q96332; Q9LPH3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Persulfide dioxygenase ETHE1 homolog, mitochondrial;
DE EC=1.13.11.18 {ECO:0000269|PubMed:22786886};
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
DE AltName: Full=Sulfur dioxygenase ETHE1;
DE Flags: Precursor;
GN Name=GLY3; OrderedLocusNames=At1g53580; ORFNames=F22G10.9, T3F20.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-294.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-294.
RC STRAIN=cv. Columbia;
RA Wintz H., Sakamoto W.;
RT "Nucleotide sequence of an Arabidopsis thaliana cDNA coding for a putative
RT glyoxalase II.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=9349270; DOI=10.1023/a:1005891123344;
RA Maiti M.K., Krishnasamy S., Owen H.A., Makaroff C.A.;
RT "Molecular characterization of glyoxalase II from Arabidopsis thaliana.";
RL Plant Mol. Biol. 35:471-481(1997).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-40, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 FUNCTION, CATALYTIC ACTIVITY, LACK OF GLYOXALATE II ACTIVITY, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22786886; DOI=10.1104/pp.112.201855;
RA Holdorf M.M., Owen H.A., Lieber S.R., Yuan L., Adams N., Dabney-Smith C.,
RA Makaroff C.A.;
RT "Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for
RT embryo and endosperm development.";
RL Plant Physiol. 160:226-236(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 51-293 IN COMPLEX WITH IRON ION,
RP SUBUNIT, AND COFACTOR.
RX PubMed=16929096; DOI=10.1107/s0907444906020592;
RA McCoy J.G., Bingman C.A., Bitto E., Holdorf M.M., Makaroff C.A.,
RA Phillips G.N. Jr.;
RT "Structure of an ETHE1-like protein from Arabidopsis thaliana.";
RL Acta Crystallogr. 62:964-970(2006).
CC -!- FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen
CC sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide
CC (H(2)S) gives rise to cysteine persulfide residues. ETHE1 consumes
CC molecular oxygen to catalyze the oxidation of the persulfide, once it
CC has been transferred to a thiophilic acceptor, such as glutathione (R-
CC SSH). Plays an important role in metabolic homeostasis in mitochondria
CC by metabolizing hydrogen sulfide and preventing the accumulation of
CC supraphysiological H(2)S levels that have toxic effects, due to the
CC inhibition of cytochrome c oxidase. Required for normal endosperm
CC development in seed, and thereby also required for normal embryo
CC development. {ECO:0000269|PubMed:22786886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) +
CC sulfite; Xref=Rhea:RHEA:12981, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905; EC=1.13.11.18;
CC Evidence={ECO:0000269|PubMed:22786886};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16929096};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16929096};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16929096}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22786886}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C8L4-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at the early heart stage, due
CC to defects in endosperm development. {ECO:0000269|PubMed:22786886}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to be a glyoxalase II isozyme
CC (PubMed:9349270), but has been shown to lack glyoxalase activity
CC (PubMed:22786886). {ECO:0000305|PubMed:22786886,
CC ECO:0000305|PubMed:9349270}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB17995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF78432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51989.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK96491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL25570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78432.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024260; AAG51989.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32965.1; -; Genomic_DNA.
DR EMBL; AY058154; AAL25570.1; ALT_INIT; mRNA.
DR EMBL; AY052298; AAK96491.1; ALT_INIT; mRNA.
DR EMBL; AY139809; AAM98115.1; -; mRNA.
DR EMBL; U74610; AAB17995.1; ALT_INIT; mRNA.
DR PIR; H96575; H96575.
DR RefSeq; NP_564636.2; NM_104236.5. [Q9C8L4-1]
DR PDB; 2GCU; X-ray; 1.48 A; A/B/C/D=51-293.
DR PDBsum; 2GCU; -.
DR AlphaFoldDB; Q9C8L4; -.
DR SMR; Q9C8L4; -.
DR BioGRID; 27018; 1.
DR STRING; 3702.AT1G53580.1; -.
DR iPTMnet; Q9C8L4; -.
DR PaxDb; Q9C8L4; -.
DR PRIDE; Q9C8L4; -.
DR ProteomicsDB; 222296; -. [Q9C8L4-1]
DR EnsemblPlants; AT1G53580.1; AT1G53580.1; AT1G53580. [Q9C8L4-1]
DR GeneID; 841793; -.
DR Gramene; AT1G53580.1; AT1G53580.1; AT1G53580. [Q9C8L4-1]
DR KEGG; ath:AT1G53580; -.
DR Araport; AT1G53580; -.
DR TAIR; locus:2024922; AT1G53580.
DR eggNOG; KOG0814; Eukaryota.
DR HOGENOM; CLU_030571_7_0_1; -.
DR InParanoid; Q9C8L4; -.
DR OMA; DYKGDTV; -.
DR OrthoDB; 1203911at2759; -.
DR BRENDA; 1.13.11.18; 399.
DR EvolutionaryTrace; Q9C8L4; -.
DR PRO; PR:Q9C8L4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8L4; baseline and differential.
DR Genevisible; Q9C8L4; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0070813; P:hydrogen sulfide metabolic process; IBA:GO_Central.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Dioxygenase; Iron;
KW Metal-binding; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 40..294
FT /note="Persulfide dioxygenase ETHE1 homolog, mitochondrial"
FT /id="PRO_0000012288"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16929096,
FT ECO:0007744|PDB:2GCU"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16929096,
FT ECO:0007744|PDB:2GCU"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16929096,
FT ECO:0007744|PDB:2GCU"
FT MOD_RES 40
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 38
FT /note="V -> L (in Ref. 4; AAB17995)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="E -> G (in Ref. 4; AAB17995)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> S (in Ref. 4; AAB17995)"
FT /evidence="ECO:0000305"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2GCU"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:2GCU"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2GCU"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:2GCU"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:2GCU"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:2GCU"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2GCU"
SQ SEQUENCE 294 AA; 32332 MW; 1C7F69EEC092DB62 CRC64;
MVMTHFSRLR QLLLLQPKFL SSQPRPLRSP PPTFLRSVMG SSSSFSSSSS KLLFRQLFEN
ESSTFTYLLA DVSHPDKPAL LIDPVDKTVD RDLKLIDELG LKLIYAMNTH VHADHVTGTG
LLKTKLPGVK SVISKASGSK ADLFLEPGDK VSIGDIYLEV RATPGHTAGC VTYVTGEGAD
QPQPRMAFTG DAVLIRGCGR TDFQEGSSDQ LYESVHSQIF TLPKDTLIYP AHDYKGFEVS
TVGEEMQHNP RLTKDKETFK TIMSNLNLSY PKMIDVAVPA NMVCGLQDVP SQAN
