ID Q5SI93_THET8 Unreviewed; 140 AA.
AC Q5SI93;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:BAD71304.1};
GN OrderedLocusNames=TTHA1481 {ECO:0000313|EMBL:BAD71304.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD71304.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0007829|PDB:1V98}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP DISULFIDE BONDS.
RA Rehse P.H., Tahirov T.H.;
RT "Crystallographic Analysis of Thioredoxin from the Thermophilic Bacteria
RT Thermus thermophilus.";
RL Submitted (JAN-2004) to the PDB data bank.
RN [2] {ECO:0000313|EMBL:BAD71304.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; AP008226; BAD71304.1; -; Genomic_DNA.
DR RefSeq; WP_011228708.1; NC_006461.1.
DR RefSeq; YP_144747.1; NC_006461.1.
DR PDB; 1V98; X-ray; 1.82 A; A/B=1-140.
DR PDBsum; 1V98; -.
DR AlphaFoldDB; Q5SI93; -.
DR SMR; Q5SI93; -.
DR EnsemblBacteria; BAD71304; BAD71304; BAD71304.
DR GeneID; 3169465; -.
DR KEGG; ttj:TTHA1481; -.
DR PATRIC; fig|300852.9.peg.1456; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_0_0; -.
DR PhylomeDB; Q5SI93; -.
DR EvolutionaryTrace; Q5SI93; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.30.30.380; Zn-finger domain of Sec23/24; 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 PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1V98};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Metal-binding {ECO:0007829|PDB:1V98};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 16..138
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:1V98"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:1V98"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:1V98"
FT DISULFID 62..65
FT /evidence="ECO:0007829|PDB:1V98"
SQ SEQUENCE 140 AA; 15162 MW; 3F21DA351BCA1DC6 CRC64;
MVVTCPKCGA KNRLGTPPPG QVPVCGACKT PLPWVVEADE KGFAQEVAGA PLTLVDFFAP
WCGPCRLVSP ILEELARDHA GRLKVVKVNV DEHPGLAARY GVRSVPTLVL FRRGAPVATW
VGASPRRVLE ERLRPYLEGR
//
