GLRX5_YEAST
ID GLRX5_YEAST Reviewed; 150 AA.
AC Q02784; D6W3V5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Monothiol glutaredoxin-5, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=GRX5 {ECO:0000312|SGD:S000005980};
GN OrderedLocusNames=YPL059W {ECO:0000312|SGD:S000005980}; ORFNames=LPE13W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11950925; DOI=10.1091/mbc.01-10-0517;
RA Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., Herrero E.;
RT "Grx5 is a mitochondrial glutaredoxin required for the activity of
RT iron/sulfur enzymes.";
RL Mol. Biol. Cell 13:1109-1121(2002).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12730244; DOI=10.1074/jbc.m303477200;
RA Tamarit J., Belli G., Cabiscol E., Herrero E., Ros J.;
RT "Biochemical characterization of yeast mitochondrial Grx5 monothiol
RT glutaredoxin.";
RL J. Biol. Chem. 278:25745-25751(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH SSQ1.
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).
RN [7]
RP FUNCTION, AND INTERACTION WITH BOL1.
RX PubMed=27532773; DOI=10.7554/elife.15991;
RA Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A.,
RA Winge D.R.;
RT "Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial
RT clients.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (PubMed:11950925, PubMed:12730244,
CC PubMed:23615440). Receives 2Fe/2S clusters from scaffold protein ISU1
CC and mediates their transfer to apoproteins, to the 4Fe/FS cluster
CC biosynthesis machinery, or export from mitochondrion (PubMed:27532773,
CC PubMed:23615440). {ECO:0000269|PubMed:11950925,
CC ECO:0000269|PubMed:12730244, ECO:0000269|PubMed:23615440,
CC ECO:0000269|PubMed:27532773}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -175 mV. {ECO:0000269|PubMed:12730244};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SSQ1
CC (PubMed:23615440). Interacts with BOL1 (PubMed:27532773).
CC {ECO:0000250|UniProtKB:Q86SX6, ECO:0000269|PubMed:23615440,
CC ECO:0000269|PubMed:27532773}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11950925}.
CC -!- MISCELLANEOUS: Present with 6260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {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; U39205; AAB68306.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11371.1; -; Genomic_DNA.
DR PIR; S60931; S60931.
DR RefSeq; NP_015266.1; NM_001183873.1.
DR PDB; 3GX8; X-ray; 1.67 A; A=30-150.
DR PDBsum; 3GX8; -.
DR AlphaFoldDB; Q02784; -.
DR SMR; Q02784; -.
DR BioGRID; 36121; 44.
DR ComplexPortal; CPX-6928; BOL1-GRX5 iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-6930; BOL3-GRX5 iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-6957; GRX5 iron-sulfur cluster assembly homodimer complex.
DR DIP; DIP-1352N; -.
DR IntAct; Q02784; 4.
DR MINT; Q02784; -.
DR STRING; 4932.YPL059W; -.
DR MaxQB; Q02784; -.
DR PaxDb; Q02784; -.
DR PRIDE; Q02784; -.
DR EnsemblFungi; YPL059W_mRNA; YPL059W; YPL059W.
DR GeneID; 856048; -.
DR KEGG; sce:YPL059W; -.
DR SGD; S000005980; GRX5.
DR VEuPathDB; FungiDB:YPL059W; -.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075082; -.
DR HOGENOM; CLU_026126_2_0_1; -.
DR InParanoid; Q02784; -.
DR OMA; KGTKLMP; -.
DR BioCyc; YEAST:G3O-33970-MON; -.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR EvolutionaryTrace; Q02784; -.
DR PRO; PR:Q02784; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02784; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:SGD.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:SGD.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IMP:SGD.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IMP:SGD.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
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; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11950925"
FT CHAIN 30..150
FT /note="Monothiol glutaredoxin-5, mitochondrial"
FT /id="PRO_0000011632"
FT DOMAIN 35..140
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 92..96
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 104
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 117..118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:3GX8"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3GX8"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3GX8"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:3GX8"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3GX8"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3GX8"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:3GX8"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3GX8"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3GX8"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:3GX8"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:3GX8"
SQ SEQUENCE 150 AA; 16931 MW; AD5FBABDF295DD04 CRC64;
MFLPKFNPIR SFSPILRAKT LLRYQNRMYL STEIRKAIED AIESAPVVLF MKGTPEFPKC
GFSRATIGLL GNQGVDPAKF AAYNVLEDPE LREGIKEFSE WPTIPQLYVN KEFIGGCDVI
TSMARSGELA DLLEEAQALV PEEEEETKDR
