ID A0A1N7APR8_9EURY Unreviewed; 89 AA.
AC A0A1N7APR8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Thiol reductase thioredoxin {ECO:0000313|EMBL:APX97912.1};
DE SubName: Full=Thioredoxin 1 {ECO:0000313|EMBL:SIR41062.1};
GN ORFNames=BB347_15560 {ECO:0000313|EMBL:APX97912.1}, SAMN05421809_1250
GN {ECO:0000313|EMBL:SIR41062.1};
OS Natronorubrum daqingense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=588898 {ECO:0000313|EMBL:SIR41062.1, ECO:0000313|Proteomes:UP000185687};
RN [1] {ECO:0000313|EMBL:APX97912.1, ECO:0000313|Proteomes:UP000187321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JX313 {ECO:0000313|EMBL:APX97912.1,
RC ECO:0000313|Proteomes:UP000187321};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIR41062.1, ECO:0000313|Proteomes:UP000185687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8909 {ECO:0000313|EMBL:SIR41062.1,
RC ECO:0000313|Proteomes:UP000185687};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP019327; APX97912.1; -; Genomic_DNA.
DR EMBL; FTNP01000001; SIR41062.1; -; Genomic_DNA.
DR RefSeq; WP_076580063.1; NZ_FTNP01000001.1.
DR AlphaFoldDB; A0A1N7APR8; -.
DR STRING; 588898.BB347_15560; -.
DR GeneID; 30957389; -.
DR KEGG; hda:BB347_15560; -.
DR OrthoDB; 35385at2157; -.
DR Proteomes; UP000185687; Unassembled WGS sequence.
DR Proteomes; UP000187321; 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 InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
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; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
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:UP000185687};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..89
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 7
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 14
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 15
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 13..16
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 89 AA; 10153 MW; 1882E42B6183453A CRC64;
MTVTLKDFYA DWCGPCKTQD PILEELEDDW EGRFEVEKVN VDEKQDVANE YQVRSLPTLV
IENDDGIVER FVGVTQRDDI EDALESAGA
//