ID K9UWP3_9CYAN Unreviewed; 243 AA.
AC K9UWP3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Glutaredoxin domain protein region {ECO:0000313|EMBL:AFY99883.1};
GN ORFNames=Cal6303_0818 {ECO:0000313|EMBL:AFY99883.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFY99883.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFY99883.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFY99883.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003610; AFY99883.1; -; Genomic_DNA.
DR RefSeq; WP_015196538.1; NC_019751.1.
DR AlphaFoldDB; K9UWP3; -.
DR STRING; 1170562.Cal6303_0818; -.
DR KEGG; calt:Cal6303_0818; -.
DR PATRIC; fig|1170562.3.peg.893; -.
DR eggNOG; COG0678; Bacteria.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_072440_2_2_3; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT DOMAIN 4..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 243 AA; 26871 MW; CBA16F9E60EACCB2 CRC64;
MLPNREGQRV PNVTFRTRRD SEWVNITTDD LFKGKTVVVF SLPGAFTPTC SSTHLPGYNQ
LAKAFHSNGV DSIVCMSVND TFVMNEWAKD QESDNVILIP DGNGEFTEGM GLLVDKTDLG
FGKRSWRYSM LVKDGIIEKM FIEPEEPGDP FKVSDADTML KYINPNAKQP ILVTLFTKVG
CPFCARAKAL LKEKGIDYEE IILGKDISTR SLKAVTAATT VPQVFIDGKL IGGSDDLAAY
FRA
//
