ID   A0A0F4PS19_PSEO7        Unreviewed;       108 AA.
AC   A0A0F4PS19;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   Name=trxA {ECO:0000313|EMBL:ATD08492.1};
GN   ORFNames=PPIS_a3760 {ECO:0000313|EMBL:ATD08492.1};
OS   Pseudoalteromonas piscicida.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43662 {ECO:0000313|EMBL:ATD08492.1, ECO:0000313|Proteomes:UP000016521};
RN   [1] {ECO:0000313|EMBL:ATD08492.1, ECO:0000313|Proteomes:UP000016521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 20779 {ECO:0000313|EMBL:ATD08492.1,
RC   ECO:0000313|Proteomes:UP000016521};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) 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; CP011924; ATD08492.1; -; Genomic_DNA.
DR   RefSeq; WP_010378172.1; NZ_PNEL01000009.1.
DR   AlphaFoldDB; A0A0F4PS19; -.
DR   STRING; 43662.TW75_03105; -.
DR   GeneID; 67500091; -.
DR   InParanoid; A0A0F4PS19; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000016521; Chromosome i.
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: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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            27
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            35
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   108 AA;  11728 MW;  F2BF6D4DCAC1A493 CRC64;
     MSDKIIQLTD DSFEADVIKS DKPVLVDFWA EWCGPCKMIA PILDEVAESH GDRVAIGKLN
     IDQNAGTPPK YGIRGIPTLL LFKDGAVAAT KVGALSKTQL VEFLENNL
//