GLRX2_SYNY3
ID GLRX2_SYNY3 Reviewed; 88 AA.
AC P73492;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Probable glutaredoxin ssr2061;
GN OrderedLocusNames=ssr2061;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P73492; Q55980: sll0662; NbExp=2; IntAct=EBI-6405758, EBI-6405750;
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17532.1; -; Genomic_DNA.
DR PIR; S77429; S77429.
DR PDB; 3QMX; X-ray; 1.82 A; A=2-88.
DR PDB; 4MJA; X-ray; 2.00 A; A=2-88.
DR PDB; 4MJB; X-ray; 2.11 A; A=2-88.
DR PDB; 4MJC; X-ray; 1.41 A; A=2-88.
DR PDB; 4MJE; X-ray; 1.20 A; A=2-88.
DR PDBsum; 3QMX; -.
DR PDBsum; 4MJA; -.
DR PDBsum; 4MJB; -.
DR PDBsum; 4MJC; -.
DR PDBsum; 4MJE; -.
DR AlphaFoldDB; P73492; -.
DR SMR; P73492; -.
DR IntAct; P73492; 2.
DR STRING; 1148.1652611; -.
DR PaxDb; P73492; -.
DR EnsemblBacteria; BAA17532; BAA17532; BAA17532.
DR KEGG; syn:ssr2061; -.
DR eggNOG; COG0695; Bacteria.
DR InParanoid; P73492; -.
DR OMA; GRTTFPQ; -.
DR PhylomeDB; P73492; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR011900; GRX_bact.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02181; GRX_bact; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..88
FT /note="Probable glutaredoxin ssr2061"
FT /id="PRO_0000141598"
FT DISULFID 15..18
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4MJE"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:4MJE"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4MJE"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:4MJE"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4MJE"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4MJE"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:4MJE"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4MJE"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:4MJE"
SQ SEQUENCE 88 AA; 9735 MW; 4F0588531B0ECCB6 CRC64;
MAVSAKIEIY TWSTCPFCMR ALALLKRKGV EFQEYCIDGD NEAREAMAAR ANGKRSLPQI
FIDDQHIGGC DDIYALDGAG KLDPLLHS