THIO_RICPR
ID THIO_RICPR Reviewed; 105 AA.
AC Q9ZEE0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=RP002;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC Participates in various redox reactions through the reversible
CC oxidation of its active center dithiol to a disulfide and catalyzes
CC dithiol-disulfide exchange reactions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA14475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ235270; CAA14475.1; ALT_INIT; Genomic_DNA.
DR PIR; D71707; D71707.
DR RefSeq; NP_220398.1; NC_000963.1.
DR RefSeq; WP_004596708.1; NC_000963.1.
DR PDB; 6MZA; NMR; -; A=1-105.
DR PDB; 6NUP; X-ray; 1.60 A; A=1-105.
DR PDBsum; 6MZA; -.
DR PDBsum; 6NUP; -.
DR AlphaFoldDB; Q9ZEE0; -.
DR BMRB; Q9ZEE0; -.
DR SMR; Q9ZEE0; -.
DR STRING; 272947.RP002; -.
DR EnsemblBacteria; CAA14475; CAA14475; CAA14475.
DR GeneID; 57569131; -.
DR KEGG; rpr:RP002; -.
DR PATRIC; fig|272947.5.peg.2; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_5; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..105
FT /note="Thioredoxin"
FT /id="PRO_0000120124"
FT DOMAIN 1..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6NUP"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:6NUP"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6NUP"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:6NUP"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:6NUP"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6NUP"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6NUP"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6NUP"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:6NUP"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6NUP"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6NUP"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6NUP"
SQ SEQUENCE 105 AA; 12057 MW; C9B1AD3BC277395C CRC64;
MVNNVTDSSF KNEVLESDLP VMVDFWAEWC GPCKMLIPII DEISKELQDK VKVLKMNIDE
NPKTPSEYGI RSIPTIMLFK NGEQKDTKIG LQQKNSLLDW INKSI
