GLRX2_RICPR
ID GLRX2_RICPR Reviewed; 107 AA.
AC O05957;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable monothiol glutaredoxin 2;
GN Name=grxC2; Synonyms=grlA; OrderedLocusNames=RP745;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA Andersson J.O., Andersson S.G.E.;
RT "Genomic rearrangements during evolution of the obligate intracellular
RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT nucleotide sequence.";
RL Microbiology 143:2783-2795(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA72459.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y11778; CAA72459.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ235273; CAA15173.1; -; Genomic_DNA.
DR PIR; E71634; E71634.
DR RefSeq; NP_221097.1; NC_000963.1.
DR RefSeq; WP_004597012.1; NC_000963.1.
DR AlphaFoldDB; O05957; -.
DR SMR; O05957; -.
DR STRING; 272947.RP745; -.
DR EnsemblBacteria; CAA15173; CAA15173; CAA15173.
DR GeneID; 57569866; -.
DR KEGG; rpr:RP745; -.
DR PATRIC; fig|272947.5.peg.778; -.
DR eggNOG; COG0278; Bacteria.
DR HOGENOM; CLU_026126_2_1_5; -.
DR OMA; KGTKLMP; -.
DR Proteomes; UP000002480; Chromosome.
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 CDD; cd03028; GRX_PICOT_like; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR014434; Monothiol_GRX.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10293; PTHR10293; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PIRSF; PIRSF005894; Monothiol_GRX; 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; Redox-active center;
KW Reference proteome.
FT CHAIN 1..107
FT /note="Probable monothiol glutaredoxin 2"
FT /id="PRO_0000102265"
FT DOMAIN 7..107
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 24
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 86..87
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 107 AA; 12003 MW; 5B77AA3E394DB4F9 CRC64;
MTKNKNLEFI QNAIKKNKVV LFMKGTKEMP ACGFSGTVVA ILNKLGVEFS DINVLFDTAL
REDLKKFSDW PTFPQLYING VLVGGCDIAK ELYQNGELEK MLKDVVV
