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Database: UniProt
Entry: A0A1V4CFW0_9BURK
LinkDB: A0A1V4CFW0_9BURK
Original site: A0A1V4CFW0_9BURK 
ID   A0A1V4CFW0_9BURK        Unreviewed;       110 AA.
AC   A0A1V4CFW0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   ORFNames=BC358_07605 {ECO:0000313|EMBL:OPF63763.1};
OS   Hydrogenophaga sp. H7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1882399 {ECO:0000313|EMBL:OPF63763.1, ECO:0000313|Proteomes:UP000189907};
RN   [1] {ECO:0000313|Proteomes:UP000189907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H7 {ECO:0000313|Proteomes:UP000189907};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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:OPF63763.1}.
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DR   EMBL; MCIC01000014; OPF63763.1; -; Genomic_DNA.
DR   RefSeq; WP_066151299.1; NZ_MCIC01000014.1.
DR   AlphaFoldDB; A0A1V4CFW0; -.
DR   STRING; 1882399.BC358_07605; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000189907; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000189907};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          3..110
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        37
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            28
FT                   /note="Deprotonates C-terminal active site Cys"
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   SITE            36
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        34..37
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   110 AA;  11865 MW;  09EB7E13BA33074E CRC64;
     MASELITHVS DATFQADVLD AKAPVLVDFW AEWCGPCKMI APILDEVAGS YNGKLKIAKV
     NVDENRDIPA KFGIRGIPTL MLFKDGQLAA TKVGAMSKAQ LTAFIDQQLA
//
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