THIO_HELPY
ID THIO_HELPY Reviewed; 106 AA.
AC P66928; P56430;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=HP_0824;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07874.1; -; Genomic_DNA.
DR PIR; H64622; H64622.
DR RefSeq; NP_207617.1; NC_000915.1.
DR RefSeq; WP_000020199.1; NC_018939.1.
DR PDB; 6BKV; X-ray; 2.35 A; A/B=1-106.
DR PDBsum; 6BKV; -.
DR AlphaFoldDB; P66928; -.
DR SMR; P66928; -.
DR IntAct; P66928; 3.
DR STRING; 85962.C694_04220; -.
DR PaxDb; P66928; -.
DR EnsemblBacteria; AAD07874; AAD07874; HP_0824.
DR KEGG; hpy:HP_0824; -.
DR PATRIC; fig|85962.47.peg.878; -.
DR eggNOG; COG3118; Bacteria.
DR OMA; KIKICKF; -.
DR PhylomeDB; P66928; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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..106
FT /note="Thioredoxin"
FT /id="PRO_0000120108"
FT DOMAIN 2..106
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 STRAND 4..6
FT /evidence="ECO:0007829|PDB:6BKV"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6BKV"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:6BKV"
FT STRAND 17..26
FT /evidence="ECO:0007829|PDB:6BKV"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:6BKV"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6BKV"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6BKV"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6BKV"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:6BKV"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6BKV"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:6BKV"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6BKV"
SQ SEQUENCE 106 AA; 11855 MW; 0616F0DC47695967 CRC64;
MSHYIELTEE NFESTIKKGV ALVDFWAPWC GPCKMLSPVI DELASEYEGK AKICKVNTDE
QEELSAKFGI RSIPTLLFTK DGEVVHQLVG VQTKVALKEQ LNKLLG