GLRX5_SCHPO
ID GLRX5_SCHPO Reviewed; 146 AA.
AC Q9HDW8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Monothiol glutaredoxin-5, mitochondrial;
GN Name=grx5 {ECO:0000312|PomBase:SPAPB2B4.02}; ORFNames=SPAPB2B4.02;
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 [GENOMIC DNA].
RA Maeng J.-H., Kim H.-G., Lim C.-J.;
RT "Cloning, expression and characterization of a monothiol glutaredoxin
RT (Grx5) from the fission yeast.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15796926; DOI=10.1016/j.bbrc.2005.02.183;
RA Chung W.H., Kim K.D., Roe J.H.;
RT "Localization and function of three monothiol glutaredoxins in
RT Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 330:604-610(2005).
RN [4]
RP INDUCTION.
RX PubMed=16258240;
RA Kim H.G., Park E.H., Lim C.J.;
RT "The fission yeast gene encoding monothiol glutaredoxin 5 is regulated by
RT nitrosative and osmotic stresses.";
RL Mol. Cells 20:43-50(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ISA1 AND ISA2.
RX PubMed=20085751; DOI=10.1016/j.bbrc.2010.01.051;
RA Kim K.D., Chung W.H., Kim H.J., Lee K.C., Roe J.H.;
RT "Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and
RT Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of
RT fission yeast.";
RL Biochem. Biophys. Res. Commun. 392:467-472(2010).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-51.
RX PubMed=23615440; DOI=10.1091/mbc.e12-09-0644;
RA Uzarska M.A., Dutkiewicz R., Freibert S.A., Lill R., Muehlenhoff U.;
RT "The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer
RT from Isu1 to Grx5 by complex formation.";
RL Mol. Biol. Cell 24:1830-1841(2013).
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (PubMed:20085751, PubMed:23615440). Receives
CC 2Fe/2S clusters from scaffold protein isu1 and mediates their transfer
CC to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export
CC from mitochondrion (PubMed:20085751, PubMed:23615440).
CC {ECO:0000269|PubMed:20085751, ECO:0000269|PubMed:23615440}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ISA1 and ISA2
CC (PubMed:20085751). {ECO:0000250|UniProtKB:Q86SX6,
CC ECO:0000269|PubMed:20085751}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15796926,
CC ECO:0000269|PubMed:20085751}.
CC -!- INDUCTION: By nitrosative and osmotic stresses.
CC {ECO:0000269|PubMed:16258240}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; AY435095; AAR08198.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC21468.1; -; Genomic_DNA.
DR RefSeq; NP_593888.1; NM_001019318.2.
DR AlphaFoldDB; Q9HDW8; -.
DR SMR; Q9HDW8; -.
DR BioGRID; 279903; 27.
DR STRING; 4896.SPAPB2B4.02.1; -.
DR MaxQB; Q9HDW8; -.
DR PaxDb; Q9HDW8; -.
DR EnsemblFungi; SPAPB2B4.02.1; SPAPB2B4.02.1:pep; SPAPB2B4.02.
DR GeneID; 2543483; -.
DR KEGG; spo:SPAPB2B4.02; -.
DR PomBase; SPAPB2B4.02; grx5.
DR VEuPathDB; FungiDB:SPAPB2B4.02; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_2_0_1; -.
DR InParanoid; Q9HDW8; -.
DR OMA; KGTKLMP; -.
DR PhylomeDB; Q9HDW8; -.
DR Reactome; R-SPO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q9HDW8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IMP:PomBase.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IGI:PomBase.
DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; ISS:PomBase.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IPI:PomBase.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10293; PTHR10293; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00365; TIGR00365; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Redox-active center; Reference proteome.
FT CHAIN 1..146
FT /note="Monothiol glutaredoxin-5, mitochondrial"
FT /id="PRO_0000102252"
FT DOMAIN 26..131
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:23615440"
FT BINDING 83..87
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 95
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 108..109
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT MUTAGEN 51
FT /note="C->S: Abolishes iron-sulfur cluster binding."
FT /evidence="ECO:0000269|PubMed:23615440"
SQ SEQUENCE 146 AA; 16533 MW; 0A48A15FDD382CDD CRC64;
MNSMFRFWIP KTSISMQLRM LSTQTRQALE QAVKEDPIVL FMKGTPTRPM CGFSLKAIQI
LSLENVASDK LVTYNVLSND ELREGIKEFS DWPTIPQLYI NGEFVGGSDI LASMHKSGEL
HKILKEINAL APEQPKDSEE ETTKKD
