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Database: UniProt
Entry: A0A0M9DTQ9_9BACT
LinkDB: A0A0M9DTQ9_9BACT
Original site: A0A0M9DTQ9_9BACT 
ID   A0A0M9DTQ9_9BACT        Unreviewed;        98 AA.
AC   A0A0M9DTQ9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:KOY86842.1};
GN   ORFNames=AD998_12445 {ECO:0000313|EMBL:KOY86842.1};
OS   bacterium 336/3.
OC   Bacteria.
OX   NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY86842.1, ECO:0000313|Proteomes:UP000037950};
RN   [1] {ECO:0000313|EMBL:KOY86842.1, ECO:0000313|Proteomes:UP000037950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:KOY86842.1,
RC   ECO:0000313|Proteomes:UP000037950};
RA   Isojarvi J., Battchikova N., Aro E.-M.;
RT   "Draft genome sequence of symbiotic bacteroides-like organism.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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:KOY86842.1}.
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DR   EMBL; LJIE01000001; KOY86842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9DTQ9; -.
DR   STRING; 1664068.AD998_12445; -.
DR   PATRIC; fig|1664068.3.peg.2533; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000037950; 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:UP000037950};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..98
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        22
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        25
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            16
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            23
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            24
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        22..25
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   98 AA;  11060 MW;  3046239367080B42 CRC64;
     MTFQEIINQD TPVLVDFYAE WCGPCKMMAP ILQEVKAEVG ETSNIIKIDV DKNPQVAQNY
     QIMGVPTLML FKNGELLWRQ SGVVPKNGLV NLLKQHIS
//
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