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 01-MAY-2013, entry version 75.
DE RecName: Full=Probable glutaredoxin ssr2061;
GN OrderedLocusNames=ssr2061;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC 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.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
CC the presence of NADPH and glutathione reductase. Reduces low
CC molecular weight disulfides and proteins (By similarity).
CC -!- INTERACTION:
CC Q55980:sll0662; NbExp=2; IntAct=EBI-6405758, EBI-6405750;
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BA000022; BAA17532.1; -; Genomic_DNA.
DR PIR; S77429; S77429.
DR RefSeq; NP_440852.1; NC_000911.1.
DR RefSeq; YP_005650911.1; NC_017277.1.
DR RefSeq; YP_007450735.1; NC_020286.1.
DR PDB; 3QMX; X-ray; 1.82 A; A=2-88.
DR PDBsum; 3QMX; -.
DR ProteinModelPortal; P73492; -.
DR SMR; P73492; 5-86.
DR IntAct; P73492; 2.
DR STRING; 1148.ssr2061; -.
DR EnsemblBacteria; BAA17532; BAA17532; BAA17532.
DR GeneID; 12254915; -.
DR GeneID; 14616387; -.
DR GeneID; 954155; -.
DR KEGG; syn:ssr2061; -.
DR KEGG; syy:SYNGTS_0958; -.
DR PATRIC; 23838944; VBISynSp132158_1037.
DR eggNOG; COG0695; -.
DR HOGENOM; HOG000095203; -.
DR KO; K03676; -.
DR OMA; IYTRQFC; -.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR011900; GRX_bact.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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; Complete proteome; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1 88 Probable glutaredoxin ssr2061.
FT /FTId=PRO_0000141598.
FT DISULFID 15 18 Redox-active (By similarity).
FT STRAND 7 11
FT HELIX 16 28
FT STRAND 33 36
FT HELIX 41 50
FT TURN 51 53
FT STRAND 59 62
FT STRAND 65 69
FT HELIX 70 78
FT HELIX 82 85
SQ SEQUENCE 88 AA; 9735 MW; 4F0588531B0ECCB6 CRC64;
MAVSAKIEIY TWSTCPFCMR ALALLKRKGV EFQEYCIDGD NEAREAMAAR ANGKRSLPQI
FIDDQHIGGC DDIYALDGAG KLDPLLHS
//
