GLRX5_LACKL
ID GLRX5_LACKL Reviewed; 143 AA.
AC Q6YFE4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Monothiol glutaredoxin-5, mitochondrial;
DE Flags: Precursor;
GN Name=GRX5; Synonyms=GRX1, PYD1-B;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18550080; DOI=10.1016/j.jmb.2008.05.029;
RA Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A.,
RA Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C.,
RA Aekerlund H.E., Gojkovic Z., Piskur J.;
RT "A second pathway to degrade pyrimidine nucleic acid precursors in
RT eukaryotes.";
RL J. Mol. Biol. 380:656-666(2008).
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (By similarity). Receives iron-sulfur clusters
CC from scaffold protein ISU1 and mediates their transfer to apoproteins,
CC to the 4Fe/FS cluster biosynthesis machinery, or export from
CC mitochondrion (By similarity). {ECO:0000250|UniProtKB:Q02784}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86SX6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q02784}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; AY154655; AAO06877.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YFE4; -.
DR SMR; Q6YFE4; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
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 3: Inferred from homology;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Redox-active center; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..143
FT /note="Monothiol glutaredoxin-5, mitochondrial"
FT /id="PRO_0000367268"
FT DOMAIN 33..138
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 58
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 90..94
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 102
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 115..116
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
SQ SEQUENCE 143 AA; 15845 MW; 04EC046EDDE8B4B7 CRC64;
MFGRISTRAL LRPAFTHRIP SVSLSRFLST ETKQAIESAI ESAPVVLFMK GTPEFPQCGF
SKATINMLGQ QGVDPMKFAA YNVLEDAELR EGVKEFSEWP TIPQLYVNKE FVGGCDIVMN
MAQTGELAKL LEDADALVPE EEE
