GenomeNet

Database: UniProt
Entry: A0A1H6QPP6_9GAMM
LinkDB: A0A1H6QPP6_9GAMM
Original site: A0A1H6QPP6_9GAMM 
ID   A0A1H6QPP6_9GAMM        Unreviewed;       287 AA.
AC   A0A1H6QPP6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:SEI42954.1};
GN   ORFNames=SAMN04487997_0603 {ECO:0000313|EMBL:SEI42954.1};
OS   Frateuria terrea.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=529704 {ECO:0000313|EMBL:SEI42954.1, ECO:0000313|Proteomes:UP000199420};
RN   [1] {ECO:0000313|EMBL:SEI42954.1, ECO:0000313|Proteomes:UP000199420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26515 {ECO:0000313|EMBL:SEI42954.1,
RC   ECO:0000313|Proteomes:UP000199420};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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; FNYC01000001; SEI42954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6QPP6; -.
DR   STRING; 529704.SAMN02927913_0519; -.
DR   Proteomes; UP000199420; 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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 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:UP000199420};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..115
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   287 AA;  31411 MW;  EBC91929338EB284 CRC64;
     MTAAAQAHVF DIDTANFETE VLRASMTTPV LVDFWATWCG PCKTLGPMLE KLAAEYNGAF
     RLGKVDVDKN QELAGMFGIR SIPTVMLVKD GQLLDGFAGA LPEGELREFL SRHVQPLEGE
     DQVEPEPAEA EDPAQTINRL QQDIAANPER SDLKLDLALA LMRNGQADTA EAELNALPAN
     LATDARAVRL RSQLDLARAL EGAPAMPELR QRVQADPADW SARDLLGVRL LLEDDPAAGL
     DQFLAILEKA RDWNDGAAKK RLLAAFATLD DAELVGHYRR RMASLLF
//
DBGET integrated database retrieval system