(data stored in ACNUC5340 zone)

SWISSPROT: GLRX2_RICCN

ID   GLRX2_RICCN             Reviewed;         107 AA.
AC   Q92GH5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Probable monothiol glutaredoxin 2;
GN   Name=grxC2; Synonyms=grlA; OrderedLocusNames=RC1148;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL03686.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AE006914; AAL03686.1; ALT_INIT; Genomic_DNA.
DR   PIR; D97843; D97843.
DR   RefSeq; WP_012151266.1; NC_003103.1.
DR   SMR; Q92GH5; -.
DR   EnsemblBacteria; AAL03686; AAL03686; RC1148.
DR   GeneID; 928288; -.
DR   KEGG; rco:RC1148; -.
DR   HOGENOM; HOG000095211; -.
DR   KO; K07390; -.
DR   OMA; KGTKLMP; -.
DR   BioCyc; RCON272944:G1FZG-1852-MONOMER; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   Gene3D; 3.40.30.10; -; 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;
DR   PRODOM; Q92GH5.
DR   SWISS-2DPAGE; Q92GH5.
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Redox-active center.
FT   CHAIN           1..107
FT                   /note="Probable monothiol glutaredoxin 2"
FT                   /id="PRO_0000102264"
FT   DOMAIN          7..107
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   REGION          86..87
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000250"
FT   METAL           32
FT                   /note="Iron-sulfur (2Fe-2S); shared with dimeric partner"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /note="Glutathione; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  12268 MW;  1A1C15F03C29D939 CRC64;
     MLENKNFKFI ENEIKNNKVV LFMKGIKKSP ACGFSGTVVA ILNKLGVEFR DINVLFDAEL
     REDLKKFSDW PTFPQLYING ELVGGCDIAR ELYQSGELEK MLKAYTR
//

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