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 27-MAR-2024, entry version 112. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00654, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q8GXX0; -. DR PaxDb; 3702-AT1G49880-1; -. 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; AT1G49880; ERV1. DR eggNOG; KOG3355; Eukaryota. DR HOGENOM; CLU_105631_0_0_1; -. DR InParanoid; Q8GXX0; -. DR OMA; GNIDIMP; -. DR OrthoDB; 1265at2759; -. DR PhylomeDB; Q8GXX0; -. DR BioCyc; ARA:AT1G49880-MONOMER; -. 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 GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro. 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; ERV/ALR sulfhydryl oxidase domain; 1. DR InterPro; IPR039799; ALR/ERV. DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf. DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase. DR PANTHER; PTHR12645; ALR/ERV; 1. DR PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1. DR Pfam; PF04777; Evr1_Alr; 1. DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1. DR PROSITE; PS51324; ERV_ALR; 1. DR Genevisible; Q8GXX0; AT. 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 //