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Database: UniProt
Entry: U5DET5_9CHRO
LinkDB: U5DET5_9CHRO
Original site: U5DET5_9CHRO 
ID   U5DET5_9CHRO            Unreviewed;       108 AA.
AC   U5DET5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   ORFNames=KR51_00033830 {ECO:0000313|EMBL:ERN40096.1};
OS   Rubidibacter lacunae KORDI 51-2.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Rubidibacter.
OX   NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN40096.1, ECO:0000313|Proteomes:UP000016960};
RN   [1] {ECO:0000313|EMBL:ERN40096.1, ECO:0000313|Proteomes:UP000016960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN40096.1,
RC   ECO:0000313|Proteomes:UP000016960};
RA   Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT   "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERN40096.1}.
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DR   EMBL; ASSJ01000081; ERN40096.1; -; Genomic_DNA.
DR   RefSeq; WP_022608990.1; NZ_ASSJ01000081.1.
DR   AlphaFoldDB; U5DET5; -.
DR   STRING; 582515.KR51_00033830; -.
DR   PATRIC; fig|582515.4.peg.3795; -.
DR   eggNOG; COG3118; Bacteria.
DR   InParanoid; U5DET5; -.
DR   OrthoDB; 530955at2; -.
DR   Proteomes; UP000016960; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016960};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   108 AA;  11956 MW;  9848D26C75CD59E8 CRC64;
     MSQAIAIADS QFDSEVLQAD KPVLVYFWAP WCGPCRLTST SIDWAAQAYA DRLKVVKMEV
     DPSPGAVKAY KVEGVPALRL LKDNEVVWSH EGALVRDKLK TNLDDHLG
//
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