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Database: UniProt
Entry: A0A1D9M8X1_9RHOB
LinkDB: A0A1D9M8X1_9RHOB
Original site: A0A1D9M8X1_9RHOB 
ID   A0A1D9M8X1_9RHOB        Unreviewed;       299 AA.
AC   A0A1D9M8X1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:AOZ68250.1};
GN   ORFNames=LPB142_02090 {ECO:0000313|EMBL:AOZ68250.1};
OS   Rhodobacter sp. LPB0142.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ68250.1, ECO:0000313|Proteomes:UP000176562};
RN   [1] {ECO:0000313|EMBL:AOZ68250.1, ECO:0000313|Proteomes:UP000176562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ68250.1,
RC   ECO:0000313|Proteomes:UP000176562};
RA   Kim E., Yi H.;
RT   "Rhodobacter sp. LPB0142, isolated from sea water.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; CP017781; AOZ68250.1; -; Genomic_DNA.
DR   RefSeq; WP_071165363.1; NZ_CP017781.1.
DR   AlphaFoldDB; A0A1D9M8X1; -.
DR   STRING; 1850250.LPB142_02090; -.
DR   KEGG; rhp:LPB142_02090; -.
DR   Proteomes; UP000176562; Chromosome.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 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   SUPFAM; SSF48452; TPR-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:UP000176562};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          3..120
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   299 AA;  31550 MW;  BB23BEC35400F42F CRC64;
     MFGTDATPAP TQLVTDVSEA NFMAEVVDKS MTVPVIVDFW APWCGPCRQL GPALEAAVQE
     AKGKVVMAKV NVDENQMIAG QMRVQSIPTV YAFWQGQPVD GFQGALPASE LKKFVEKLAA
     LAGDGGLADA VAAAEEMLAE GAAVDAAETF AAILEEDGEN AEAYGGLVRA HLALGNLDQA
     EAFLAGVPAK IAASAPVEAA RAQVALARQA EKAGPLDALK SAVEADPADA QARFDYAQAL
     HAGGQIEEAV DQLLELFRRD REWNEGAAKT QLFTIFDALK PNDPIVLKGR RKLSSMVFA
//
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