GenomeNet

Database: UniProt
Entry: A0A433WAH3_9BACT
LinkDB: A0A433WAH3_9BACT
Original site: A0A433WAH3_9BACT 
ID   A0A433WAH3_9BACT        Unreviewed;        99 AA.
AC   A0A433WAH3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:NSL86737.1};
GN   Name=trxA {ECO:0000313|EMBL:NSL86737.1};
GN   ORFNames=ECE50_007845 {ECO:0000313|EMBL:NSL86737.1};
OS   Chitinophaga solisilvae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1233460 {ECO:0000313|EMBL:NSL86737.1, ECO:0000313|Proteomes:UP000281028};
RN   [1] {ECO:0000313|EMBL:NSL86737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mgbs1 {ECO:0000313|EMBL:NSL86737.1};
RA   Goh C.B.S., Lee M.S., Parimannan S., Pasbakhsh P., Yule C.M., Rajandas H.,
RA   Loke S., Croft L., Tan J.B.L.;
RT   "Chitinophaga laudate sp. nov., isolated from a tropical peat swamp.";
RL   Submitted (MAY-2020) 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:NSL86737.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RIAR02000001; NSL86737.1; -; Genomic_DNA.
DR   Proteomes; UP000281028; 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:UP000281028};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   ACT_SITE        23
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        26
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            17
FT                   /note="Deprotonates C-terminal active site Cys"
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   SITE            25
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   99 AA;  11250 MW;  28CD12F5BE125006 CRC64;
     MENLQAILQS ATPVLIDCFA TWCGPCKMVP PILKEVKDKF GESLRIIKID IDRNQQLSAQ
     WQISSVPTLL LFREGRLLWR QSGVVPAHQL IPLLQQQLS
//
DBGET integrated database retrieval system