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Monothiol glutaredoxin-5, mitochondrial

 GLRX5_YEAST             Reviewed;         150 AA.
Q02784; D6W3V5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 157.
RecName: Full=Monothiol glutaredoxin-5, mitochondrial;
Flags: Precursor;
Name=GRX5; OrderedLocusNames=YPL059W; ORFNames=LPE13W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11950925; DOI=10.1091/mbc.01-10-0517;
Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., Herrero E.;
"Grx5 is a mitochondrial glutaredoxin required for the activity of
iron/sulfur enzymes.";
Mol. Biol. Cell 13:1109-1121(2002).
[4]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12730244; DOI=10.1074/jbc.M303477200;
Tamarit J., Belli G., Cabiscol E., Herrero E., Ros J.;
"Biochemical characterization of yeast mitochondrial Grx5 monothiol
glutaredoxin.";
J. Biol. Chem. 278:25745-25751(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
FUNCTION, AND INTERACTION WITH BOL1.
PubMed=27532773; DOI=10.7554/eLife.15991;
Melber A., Na U., Vashisht A., Weiler B.D., Lill R.,
Wohlschlegel J.A., Winge D.R.;
"Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to
mitochondrial clients.";
Elife 5:0-0(2016).
-!- FUNCTION: Monothiol glutaredoxin involved in iron-sulfur
biogenesis (PubMed:11950925, PubMed:12730244). Required for normal
iron homeostasis (PubMed:11950925, PubMed:12730244). Protects
cells against oxidative damage due to reactive oxygen species
(PubMed:12730244). Collaborates with BOL1 in iron-sulfur protein
assembly when the iron-sulfur cluster is inserted into the target
protein (PubMed:27532773). {ECO:0000269|PubMed:11950925,
ECO:0000269|PubMed:12730244, ECO:0000269|PubMed:27532773}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E(0) is -175 mV. {ECO:0000269|PubMed:12730244};
-!- SUBUNIT: Homodimer (By similarity). Interacts with BOL1
(PubMed:27532773). {ECO:0000250, ECO:0000269|PubMed:27532773}.
-!- INTERACTION:
P32561:RPD3; NbExp=3; IntAct=EBI-29427, EBI-15864;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11950925}.
-!- MISCELLANEOUS: Present with 6260 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U39205; AAB68306.1; -; Genomic_DNA.
EMBL; BK006949; DAA11371.1; -; Genomic_DNA.
PIR; S60931; S60931.
RefSeq; NP_015266.1; NM_001183873.1.
PDB; 3GX8; X-ray; 1.67 A; A=30-150.
PDBsum; 3GX8; -.
ProteinModelPortal; Q02784; -.
SMR; Q02784; -.
BioGrid; 36121; 42.
DIP; DIP-1352N; -.
IntAct; Q02784; 11.
MINT; Q02784; -.
STRING; 4932.YPL059W; -.
MaxQB; Q02784; -.
PaxDb; Q02784; -.
PRIDE; Q02784; -.
EnsemblFungi; YPL059W; YPL059W; YPL059W.
GeneID; 856048; -.
KEGG; sce:YPL059W; -.
EuPathDB; FungiDB:YPL059W; -.
SGD; S000005980; GRX5.
GeneTree; ENSGT00550000075082; -.
HOGENOM; HOG000095211; -.
InParanoid; Q02784; -.
KO; K07390; -.
OMA; KGTKLMP; -.
OrthoDB; EOG092C3TIP; -.
BioCyc; YEAST:G3O-33970-MONOMER; -.
Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
EvolutionaryTrace; Q02784; -.
PRO; PR:Q02784; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:SGD.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
CDD; cd03028; GRX_PICOT_like; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR014434; Monothiol_GRX.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 1.
PIRSF; PIRSF005894; Monothiol_GRX; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Direct protein sequencing;
Iron; Iron-sulfur; Metal-binding; Mitochondrion; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 29 Mitochondrion.
{ECO:0000269|PubMed:11950925}.
CHAIN 30 150 Monothiol glutaredoxin-5, mitochondrial.
/FTId=PRO_0000011632.
DOMAIN 35 140 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 92 96 Glutathione binding. {ECO:0000250}.
REGION 117 118 Glutathione binding. {ECO:0000250}.
METAL 60 60 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250}.
BINDING 52 52 Glutathione. {ECO:0000250}.
BINDING 104 104 Glutathione; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
HELIX 32 43 {ECO:0000244|PDB:3GX8}.
STRAND 46 53 {ECO:0000244|PDB:3GX8}.
STRAND 55 58 {ECO:0000244|PDB:3GX8}.
HELIX 62 73 {ECO:0000244|PDB:3GX8}.
HELIX 77 79 {ECO:0000244|PDB:3GX8}.
STRAND 80 84 {ECO:0000244|PDB:3GX8}.
HELIX 89 99 {ECO:0000244|PDB:3GX8}.
STRAND 106 109 {ECO:0000244|PDB:3GX8}.
STRAND 112 116 {ECO:0000244|PDB:3GX8}.
HELIX 117 126 {ECO:0000244|PDB:3GX8}.
HELIX 128 135 {ECO:0000244|PDB:3GX8}.
SEQUENCE 150 AA; 16931 MW; AD5FBABDF295DD04 CRC64;
MFLPKFNPIR SFSPILRAKT LLRYQNRMYL STEIRKAIED AIESAPVVLF MKGTPEFPKC
GFSRATIGLL GNQGVDPAKF AAYNVLEDPE LREGIKEFSE WPTIPQLYVN KEFIGGCDVI
TSMARSGELA DLLEEAQALV PEEEEETKDR


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