THIO_ECO57
ID THIO_ECO57 Reviewed; 109 AA.
AC P0AA27; P00274; P76750; Q47674; Q8XAT2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Thioredoxin 1;
DE Short=Trx-1;
GN Name=trxA; OrderedLocusNames=Z5291, ECs4714;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58975.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB38137.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58975.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38137.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_312741.1; NC_002695.1.
DR RefSeq; WP_001280776.1; NZ_SWKA01000005.1.
DR PDB; 3DXB; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-109.
DR PDB; 5E4W; X-ray; 2.80 A; A/B=3-109.
DR PDB; 5IKN; X-ray; 4.80 A; K/L/M=4-108.
DR PDBsum; 3DXB; -.
DR PDBsum; 5E4W; -.
DR PDBsum; 5IKN; -.
DR AlphaFoldDB; P0AA27; -.
DR BMRB; P0AA27; -.
DR SMR; P0AA27; -.
DR STRING; 155864.EDL933_5101; -.
DR PRIDE; P0AA27; -.
DR EnsemblBacteria; AAG58975; AAG58975; Z5291.
DR EnsemblBacteria; BAB38137; BAB38137; ECs_4714.
DR GeneID; 64173577; -.
DR GeneID; 67514182; -.
DR GeneID; 915255; -.
DR KEGG; ece:Z5291; -.
DR KEGG; ecs:ECs_4714; -.
DR PATRIC; fig|386585.9.peg.4918; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_6; -.
DR OMA; QVGVAPK; -.
DR EvolutionaryTrace; P0AA27; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; Acetylation; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..109
FT /note="Thioredoxin 1"
FT /id="PRO_0000120098"
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 27
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5E4W"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3DXB"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:3DXB"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:3DXB"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:3DXB"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3DXB"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3DXB"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3DXB"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:3DXB"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3DXB"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:3DXB"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:3DXB"
SQ SEQUENCE 109 AA; 11807 MW; EF5933EA29668EE9 CRC64;
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN
IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA
