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Database: UniProt
Entry: G7USM3_PSEUP
LinkDB: G7USM3_PSEUP
Original site: G7USM3_PSEUP 
ID   G7USM3_PSEUP            Unreviewed;       146 AA.
AC   G7USM3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:AER57274.1};
GN   OrderedLocusNames=DSC_13150 {ECO:0000313|EMBL:AER57274.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57274.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER57274.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER57274.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; CP003093; AER57274.1; -; Genomic_DNA.
DR   RefSeq; WP_014161447.1; NC_016147.2.
DR   AlphaFoldDB; G7USM3; -.
DR   STRING; 1045855.DSC_13150; -.
DR   KEGG; psd:DSC_13150; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_090389_10_0_6; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000005870; Chromosome.
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   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR049299; Thio2_N.
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; PF21352; Thio2_N; 1.
DR   Pfam; PF00085; 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          33..145
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   146 AA;  15944 MW;  3E33A4309E399625 CRC64;
     MSEPLLIACP HCHARNRVPE QRLGQGPACG RCHQALFTAH PLALDAAHFD THARDSDLPL
     LVDFWAPWCG PCKMMAPHFE AAAAQLEPQL RLAKVDTEAH PALGARFGIR SIPTMAVFLH
     GRELGRQSGA MQQADIVRWA RATAGL
//
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