THIO1_STRCO
ID THIO1_STRCO Reviewed; 110 AA.
AC P52230;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 4.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Thioredoxin 1;
DE Short=Trx-1;
GN Name=trxA; OrderedLocusNames=SCO3889; ORFNames=SCH24.11c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9795152; DOI=10.1016/s0378-1119(98)00357-6;
RA Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y.;
RT "Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor
RT chromosome and comparison with other eubacteria.";
RL Gene 217:83-90(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=10671452; DOI=10.1128/jb.182.5.1313-1320.2000;
RA Kim H.-J., Calcutt M.J., Schmidt F.J., Chater K.F.;
RT "Partitioning of the linear chromosome during sporulation of Streptomyces
RT coelicolor A3(2) involves an oriC-linked parAB locus.";
RL J. Bacteriol. 182:1313-1320(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9755177; DOI=10.1093/emboj/17.19.5776;
RA Paget M.S., Kang J.G., Roe J.H., Buttner M.J.;
RT "sigmaR, an RNA polymerase sigma factor that modulates expression of the
RT thioredoxin system in response to oxidative stress in Streptomyces
RT coelicolor A3(2).";
RL EMBO J. 17:5776-5782(1998).
RN [5]
RP FUNCTION WITH RSRA AS SUBSTRATE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10428967; DOI=10.1093/emboj/18.15.4292;
RA Kang J.G., Paget M.S.B., Seok Y.J., Hahn M.Y., Bae J.B., Hahn J.S.;
RT "RsrA, an anti-sigma factor regulated by redox change.";
RL EMBO J. 18:4292-4298(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS).
RX PubMed=16510983; DOI=10.1107/s1744309104032993;
RA Stefankova P., Maderova J., Barak I., Kollarova M., Otwinowski Z.;
RT "Expression, purification and X-ray crystallographic analysis of
RT thioredoxin from Streptomyces coelicolor.";
RL Acta Crystallogr. F 61:164-168(2005).
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. Stimulates complex formation
CC between sigma factor SigR and its cognate anti-sigma factor RsrA
CC probably by reducing RsrA. {ECO:0000269|PubMed:10428967}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed from 2 promoters, 1 of which (trxBp1) is under
CC control of SigR, and further transiently induced (about 50-fold) by the
CC thiol-oxidizing agent diamide. Part of the trxB-trxA operon.
CC {ECO:0000269|PubMed:9755177}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; X92105; CAA63077.1; -; Genomic_DNA.
DR EMBL; X92103; CAA63074.1; -; Genomic_DNA.
DR EMBL; AJ007313; CAA07452.1; -; Genomic_DNA.
DR EMBL; AF031590; AAC03481.1; -; Genomic_DNA.
DR EMBL; AF187159; AAF16002.1; -; Genomic_DNA.
DR EMBL; AL939118; CAB42711.1; -; Genomic_DNA.
DR PIR; T36576; T36576.
DR PIR; T42061; T42061.
DR RefSeq; NP_628075.1; NC_003888.3.
DR RefSeq; WP_003975042.1; NZ_VNID01000003.1.
DR PDB; 1T00; X-ray; 1.51 A; A=1-110.
DR PDBsum; 1T00; -.
DR AlphaFoldDB; P52230; -.
DR SMR; P52230; -.
DR STRING; 100226.SCO3889; -.
DR GeneID; 1099325; -.
DR KEGG; sco:SCO3889; -.
DR PATRIC; fig|100226.15.peg.3962; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_11; -.
DR InParanoid; P52230; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P52230; -.
DR EvolutionaryTrace; P52230; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
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; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..110
FT /note="Thioredoxin 1"
FT /id="PRO_0000120136"
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 95..96
FT /note="KP -> NA (in Ref. 1; CAA63074/CAA07452)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1T00"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1T00"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1T00"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1T00"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1T00"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:1T00"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1T00"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1T00"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1T00"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1T00"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1T00"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1T00"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:1T00"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1T00"
SQ SEQUENCE 110 AA; 11892 MW; 18AA0F89F7E513A8 CRC64;
MAGTLKHVTD DSFEQDVLKN DKPVLVDFWA AWCGPCRQIA PSLEAIAAEY GDKIEIVKLN
IDENPGTAAK YGVMSIPTLN VYQGGEVAKT IVGAKPKAAI VRDLEDFIAD
