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Database: UniProt
Entry: A0A1Z4VUF8_9GAMM
LinkDB: A0A1Z4VUF8_9GAMM
Original site: A0A1Z4VUF8_9GAMM 
ID   A0A1Z4VUF8_9GAMM        Unreviewed;       125 AA.
AC   A0A1Z4VUF8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   ORFNames=FOKN1_2452 {ECO:0000313|EMBL:BAZ94824.1};
OS   Thiohalobacter thiocyanaticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalobacterales;
OC   Thiohalobacteraceae; Thiohalobacter.
OX   NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ94824.1, ECO:0000313|Proteomes:UP000218765};
RN   [1] {ECO:0000313|EMBL:BAZ94824.1, ECO:0000313|Proteomes:UP000218765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ94824.1,
RC   ECO:0000313|Proteomes:UP000218765};
RA   Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT   "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; AP018052; BAZ94824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4VUF8; -.
DR   KEGG; ttc:FOKN1_2452; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000218765; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF40; THIOREDOXIN 2; 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   Isomerase {ECO:0000313|EMBL:BAZ94824.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218765};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..120
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        30
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            24
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            31
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            32
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        30..33
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   125 AA;  14436 MW;  1F4B77EBBCFF955D CRC64;
     MATVELTKEN FEQIITDNDF VLIDFWAEWC GPCKNFAPIF EEASEKYPDI VFAKVDTEAQ
     QELAAYFQIR SIPTLMIFRE RVIIFSQPGM LPGSALDELI GKAKELDMDQ VRKEIEEQQQ
     NQQQG
//
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