ERV1_SCHPO
ID ERV1_SCHPO Reviewed; 182 AA.
AC O14144;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Mitochondrial FAD-linked sulfhydryl oxidase erv1;
DE EC=1.8.3.2;
GN Name=erv1; ORFNames=SPAC3G6.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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) (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00654}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}.
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DR EMBL; CU329670; CAB16284.1; -; Genomic_DNA.
DR PIR; T38727; T38727.
DR RefSeq; NP_594974.1; NM_001020405.2.
DR AlphaFoldDB; O14144; -.
DR SMR; O14144; -.
DR STRING; 4896.SPAC3G6.08.1; -.
DR MaxQB; O14144; -.
DR PaxDb; O14144; -.
DR PRIDE; O14144; -.
DR EnsemblFungi; SPAC3G6.08.1; SPAC3G6.08.1:pep; SPAC3G6.08.
DR GeneID; 2543175; -.
DR KEGG; spo:SPAC3G6.08; -.
DR PomBase; SPAC3G6.08; erv1.
DR VEuPathDB; FungiDB:SPAC3G6.08; -.
DR eggNOG; KOG3355; Eukaryota.
DR HOGENOM; CLU_070631_1_0_1; -.
DR InParanoid; O14144; -.
DR OMA; PCRTCNT; -.
DR PhylomeDB; O14144; -.
DR PRO; PR:O14144; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISO:PomBase.
DR GO; GO:0006457; P:protein folding; ISO:PomBase.
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 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..182
FT /note="Mitochondrial FAD-linked sulfhydryl oxidase erv1"
FT /id="PRO_0000339121"
FT DOMAIN 75..177
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT BINDING 81..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 153..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT BINDING 176..177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P55789"
FT DISULFID 122..125
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 153..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ SEQUENCE 182 AA; 20769 MW; C8756CB2022F4746 CRC64;
MVFGKRYRDK ETGIIYDENG RPCKTCNIFS SFRNVAQQPN SSTVPEVKSN TQLESKQSSI
DCNTNAIPDS VSFPRLPDVA ELGRSTWTFL HAMAANFPKN PTPTQQNDMS SFLYNFSKFY
PCWSCAEDLR IWMAKYGNSP RVDSRESLCE WICEAHNDVN ERLGKPLFNC QVWSKKASEL
AD
