ERV1_YEAST
ID ERV1_YEAST Reviewed; 189 AA.
AC P27882; D6VUG4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Mitochondrial FAD-linked sulfhydryl oxidase ERV1;
DE EC=1.8.3.2 {ECO:0000305|PubMed:10899311};
DE AltName: Full=14 kDa regulatory protein;
DE AltName: Full=Essential for respiration and vegetative growth protein 1;
GN Name=ERV1; OrderedLocusNames=YGR029W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC167;
RX PubMed=1552903; DOI=10.1007/bf00299137;
RA Lisowsky T.;
RT "Dual function of a new nuclear gene for oxidative phosphorylation and
RT vegetative growth in yeast.";
RL Mol. Gen. Genet. 232:58-64(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SF747-19D;
RX PubMed=8226973; DOI=10.1016/s0021-9258(20)80519-5;
RA Nakai M., Endo T., Hase T., Matsubara H.;
RT "Intramitochondrial protein sorting. Isolation and characterization of the
RT yeast MSP1 gene which belongs to a novel family of putative ATPases.";
RL J. Biol. Chem. 268:24262-24269(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP REVISION OF GENE MODEL.
RX PubMed=8972573;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1501::aid-yea40>3.0.co;2-h;
RA Lisowsky T.;
RT "Removal of an intron with unique 3' branch site creates an amino-terminal
RT protein sequence directing the scERV1 gene product to mitochondria.";
RL Yeast 12:1501-1510(1996).
RN [7]
RP FUNCTION, FAD-BINDING, AND CATALYTIC ACTIVITY.
RX PubMed=10899311; DOI=10.1016/s0014-5793(00)01767-1;
RA Lee J.-E., Hofhaus G., Lisowsky T.;
RT "Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase.";
RL FEBS Lett. 477:62-66(2000).
RN [8]
RP FUNCTION, MUTAGENESIS OF CYS-30; CYS-33; CYS-130; CYS-133; CYS-159 AND
RP CYS-176, AND SUBUNIT.
RX PubMed=12654008; DOI=10.1046/j.1432-1033.2003.03519.x;
RA Hofhaus G., Lee J.E., Tews I., Rosenberg B., Lisowsky T.;
RT "The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is
RT essential for in vivo activity and interacts with the primary redox
RT centre.";
RL Eur. J. Biochem. 270:1528-1535(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11493598; DOI=10.1093/embo-reports/kve161;
RA Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., Lill R.;
RT "An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in
RT the maturation of cytosolic Fe/S proteins.";
RL EMBO Rep. 2:715-720(2001).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH MIA40.
RX PubMed=15989955; DOI=10.1016/j.cell.2005.04.011;
RA Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K.,
RA Herrmann J.M.;
RT "A disulfide relay system in the intermembrane space of mitochondria that
RT mediates protein import.";
RL Cell 121:1059-1069(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH MIA40.
RX PubMed=16181637; DOI=10.1016/j.jmb.2005.08.051;
RA Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B.,
RA Pfanner N., Chacinska A.;
RT "The essential mitochondrial protein Erv1 cooperates with Mia40 in
RT biogenesis of intermembrane space proteins.";
RL J. Mol. Biol. 353:485-492(2005).
RN [13]
RP FUNCTION.
RX PubMed=16185707; DOI=10.1016/j.jmb.2005.08.049;
RA Allen S., Balabanidou V., Sideris D.P., Lisowsky T., Tokatlidis K.;
RT "Erv1 mediates the Mia40-dependent protein import pathway and provides a
RT functional link to the respiratory chain by shuttling electrons to
RT cytochrome c.";
RL J. Mol. Biol. 353:937-944(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC bond formation. Required for the import and folding of small cysteine-
CC containing proteins in the mitochondrial intermembrane space (IMS).
CC Forms a redox cycle with MIA40 that involves a disulfide relay system.
CC Important for maintaining the cysteine residues in MIA40 in an oxidized
CC state. Reduced ERV1 is reoxidized by cytochrome c. Required for the
CC maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
CC {ECO:0000255|PROSITE-ProRule:PRU00654, ECO:0000269|PubMed:10899311,
CC ECO:0000269|PubMed:11493598, ECO:0000269|PubMed:12654008,
CC ECO:0000269|PubMed:15989955, ECO:0000269|PubMed:16181637,
CC ECO:0000269|PubMed:16185707}.
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 Evidence={ECO:0000305|PubMed:10899311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17358;
CC Evidence={ECO:0000305|PubMed:10899311};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654,
CC ECO:0000269|PubMed:10899311};
CC -!- SUBUNIT: Homodimer. Interacts with MIA40, forming transient
CC intermolecular disulfide bridges. {ECO:0000269|PubMed:12654008,
CC ECO:0000269|PubMed:15989955, ECO:0000269|PubMed:16181637}.
CC -!- INTERACTION:
CC P27882; P36046: MIA40; NbExp=4; IntAct=EBI-6621, EBI-26978;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:11493598, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:22984289}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB48659.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA43129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA48192.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X60722; CAA43129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M74772; AAB48659.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X68055; CAA48192.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72814; CAA97017.1; -; Genomic_DNA.
DR EMBL; Z72813; CAA97016.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08125.1; -; Genomic_DNA.
DR PIR; S20469; S20469.
DR RefSeq; NP_011543.4; NM_001181158.3.
DR PDB; 3W4Y; X-ray; 2.00 A; A/B/C=73-189.
DR PDB; 4E0H; X-ray; 2.00 A; A=86-189.
DR PDB; 4E0I; X-ray; 3.00 A; A/B/C=1-189.
DR PDBsum; 3W4Y; -.
DR PDBsum; 4E0H; -.
DR PDBsum; 4E0I; -.
DR AlphaFoldDB; P27882; -.
DR SMR; P27882; -.
DR BioGRID; 33273; 31.
DR IntAct; P27882; 5.
DR MINT; P27882; -.
DR STRING; 4932.YGR029W; -.
DR CarbonylDB; P27882; -.
DR MaxQB; P27882; -.
DR PaxDb; P27882; -.
DR PRIDE; P27882; -.
DR EnsemblFungi; YGR029W_mRNA; YGR029W; YGR029W.
DR GeneID; 852916; -.
DR KEGG; sce:YGR029W; -.
DR SGD; S000003261; ERV1.
DR VEuPathDB; FungiDB:YGR029W; -.
DR eggNOG; KOG3355; Eukaryota.
DR GeneTree; ENSGT00390000001979; -.
DR HOGENOM; CLU_070631_1_0_1; -.
DR InParanoid; P27882; -.
DR OMA; NCDLWKK; -.
DR BioCyc; YEAST:G3O-30753-MON; -.
DR BRENDA; 1.8.3.2; 984.
DR PRO; PR:P27882; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P27882; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IDA:SGD.
DR GO; GO:0016972; F:thiol oxidase activity; IMP:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:SGD.
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..189
FT /note="Mitochondrial FAD-linked sulfhydryl oxidase ERV1"
FT /id="PRO_0000001187"
FT DOMAIN 83..183
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT BINDING 88..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 159..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 182..183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT DISULFID 130..133
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 159..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT MUTAGEN 30
FT /note="C->S: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:12654008"
FT MUTAGEN 33
FT /note="C->S: Reduces catalytic activity 2-fold."
FT /evidence="ECO:0000269|PubMed:12654008"
FT MUTAGEN 130
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:12654008"
FT MUTAGEN 133
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:12654008"
FT MUTAGEN 159
FT /note="C->S: Reduces catalytic activity 3.3-fold."
FT /evidence="ECO:0000269|PubMed:12654008"
FT MUTAGEN 176
FT /note="C->S: Reduces catalytic activity 2.6-fold."
FT /evidence="ECO:0000269|PubMed:12654008"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:4E0I"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4E0I"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:4E0I"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4E0I"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:3W4Y"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:3W4Y"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:3W4Y"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:3W4Y"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3W4Y"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:3W4Y"
SQ SEQUENCE 189 AA; 21639 MW; 83DADA0DB1DF17CC CRC64;
MKAIDKMTDN PPQEGLSGRK IIYDEDGKPC RSCNTLLDFQ YVTGKISNGL KNLSSNGKLA
GTGALTGEAS ELMPGSRTYR KVDPPDVEQL GRSSWTLLHS VAASYPAQPT DQQKGEMKQF
LNIFSHIYPC NWCAKDFEKY IRENAPQVES REELGRWMCE AHNKVNKKLR KPKFDCNFWE
KRWKDGWDE
