ERV1_ARATH
ID ERV1_ARATH Reviewed; 191 AA.
AC Q8GXX0; Q8LC15; Q9C6C6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=FAD-linked sulfhydryl oxidase ERV1;
DE Short=AtErv1;
DE EC=1.8.3.2;
DE AltName: Full=Mitochondrial sulfhydryl oxidase ERV1;
GN Name=ERV1; OrderedLocusNames=At1g49880; ORFNames=F10F5.3;
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, COFACTOR, SUBUNIT, SUBCELLULAR
RP LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=14996837; DOI=10.1074/jbc.m312877200;
RA Levitan A., Danon A., Lisowsky T.;
RT "Unique features of plant mitochondrial sulfhydryl oxidase.";
RL J. Biol. Chem. 279:20002-20008(2004).
RN [2]
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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20829360; DOI=10.1074/jbc.m110.121202;
RA Carrie C., Giraud E., Duncan O., Xu L., Wang Y., Huang S., Clifton R.,
RA Murcha M., Filipovska A., Rackham O., Vrielink A., Whelan J.;
RT "Conserved and novel functions for Arabidopsis thaliana MIA40 in assembly
RT of proteins in mitochondria and peroxisomes.";
RL J. Biol. Chem. 285:36138-36148(2010).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=19017646; DOI=10.1074/jbc.m806316200;
RA Farver O., Vitu E., Wherland S., Fass D., Pecht I.;
RT "Electron transfer reactivity of the Arabidopsis thaliana sulfhydryl
RT oxidase AtErv1.";
RL J. Biol. Chem. 284:2098-2105(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 71-191 IN COMPLEX WITH FAD,
RP SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-177 AND CYS-182, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=16893552; DOI=10.1016/j.jmb.2006.06.070;
RA Vitu E., Bentzur M., Lisowsky T., Kaiser C.A., Fass D.;
RT "Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering
RT of the shuttle disulfide.";
RL J. Mol. Biol. 362:89-101(2006).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC bond formation (PubMed:14996837, PubMed:16893552). Oxidizes thioredoxin
CC in vitro (PubMed:14996837, PubMed:16893552). Required for the import
CC and folding of small cysteine-containing proteins in the mitochondrial
CC intermembrane space. Forms a redox cycle with MIA40 that involves a
CC disulfide relay system. Important for maintaining the cysteine residues
CC in MIA40 in an oxidized state (By similarity).
CC {ECO:0000250|UniProtKB:P27882, ECO:0000305|PubMed:14996837,
CC ECO:0000305|PubMed:16893552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17358;
CC Evidence={ECO:0000305|PubMed:14996837, ECO:0000305|PubMed:16893552};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654,
CC ECO:0000269|PubMed:14996837};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14996837,
CC ECO:0000269|PubMed:16893552}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14996837}.
CC -!- PTM: Contains three disulfide bonds; one catalytic disulfide (Cys-119
CC to Cys-122), one structural disulfide (Cys-148 to Cys-165), and one
CC shuttle disulfide (Cys-177 to Cys-182). {ECO:0000269|PubMed:19017646}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:16893552}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ551263; CAD83013.1; -; mRNA.
DR EMBL; AC079674; AAG51780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32487.1; -; Genomic_DNA.
DR EMBL; AK117991; BAC42626.1; -; mRNA.
DR EMBL; BT003718; AAO39946.1; -; mRNA.
DR EMBL; AY086861; AAM63908.1; -; mRNA.
DR PIR; G96535; G96535.
DR RefSeq; NP_564557.1; NM_103875.4.
DR PDB; 2HJ3; X-ray; 2.50 A; A/B=71-191.
DR PDBsum; 2HJ3; -.
DR AlphaFoldDB; Q8GXX0; -.
DR SMR; Q8GXX0; -.
DR BioGRID; 26636; 1.
DR STRING; 3702.AT1G49880.1; -.
DR PaxDb; Q8GXX0; -.
DR PRIDE; Q8GXX0; -.
DR ProteomicsDB; 220643; -.
DR EnsemblPlants; AT1G49880.1; AT1G49880.1; AT1G49880.
DR GeneID; 841411; -.
DR Gramene; AT1G49880.1; AT1G49880.1; AT1G49880.
DR KEGG; ath:AT1G49880; -.
DR Araport; AT1G49880; -.
DR TAIR; locus:2007283; AT1G49880.
DR eggNOG; KOG3355; Eukaryota.
DR HOGENOM; CLU_105631_0_0_1; -.
DR InParanoid; Q8GXX0; -.
DR OMA; TFPCERV; -.
DR OrthoDB; 1537996at2759; -.
DR PhylomeDB; Q8GXX0; -.
DR BioCyc; ARA:AT1G49880-MON; -.
DR BRENDA; 1.8.3.2; 399.
DR EvolutionaryTrace; Q8GXX0; -.
DR PRO; PR:Q8GXX0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GXX0; baseline and differential.
DR Genevisible; Q8GXX0; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0016972; F:thiol oxidase activity; IDA:UniProtKB.
DR DisProt; DP02648; -.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; PTHR12645; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..191
FT /note="FAD-linked sulfhydryl oxidase ERV1"
FT /id="PRO_0000401377"
FT DOMAIN 72..172
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT MOTIF 177..182
FT /note="Required for dimerization and substrate specificity"
FT BINDING 76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT BINDING 81..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT BINDING 121..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT BINDING 148..155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT BINDING 171..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16893552"
FT DISULFID 119..122
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:19017646"
FT DISULFID 148..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:16893552, ECO:0000269|PubMed:19017646"
FT DISULFID 177..182
FT /evidence="ECO:0000269|PubMed:16893552,
FT ECO:0000269|PubMed:19017646"
FT MUTAGEN 177
FT /note="C->A: Loss the capacity to oxidize thioredoxin; when
FT associated with A-182."
FT /evidence="ECO:0000269|PubMed:16893552"
FT MUTAGEN 182
FT /note="C->A: Loss the capacity to oxidize thioredoxin; when
FT associated with A-177."
FT /evidence="ECO:0000269|PubMed:16893552"
FT CONFLICT 35..36
FT /note="PS -> R (in Ref. 6; AAM63908)"
FT /evidence="ECO:0000305"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:2HJ3"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:2HJ3"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:2HJ3"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:2HJ3"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:2HJ3"
SQ SEQUENCE 191 AA; 21600 MW; 7CC7FEA44C0D4B38 CRC64;
MGEKPWQPLL QSFEKLSNCV QTHLSNFIGI KNTPPSSQST IQNPIISLDS SPPIATNSSS
LQKLPLKDKS TGPVTKEDLG RATWTFLHTL AAQYPEKPTR QQKKDVKELM TILSRMYPCR
ECADHFKEIL RSNPAQAGSQ EEFSQWLCHV HNTVNRSLGK LVFPCERVDA RWGKLECEQK
SCDLHGTSMD F
