THIO_CHLAA
ID THIO_CHLAA Reviewed; 110 AA.
AC Q7M1B9; A9WI56;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=Caur_2541;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [2]
RP PROTEIN SEQUENCE OF 2-110, MASS SPECTROMETRY, AND METHYLATION AT LYS-105.
RA Biemann K., Papayannopoulos I.A.;
RT "Amino acid sequencing of proteins.";
RL Acc. Chem. Res. 27:370-378(1994).
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.
CC -!- MASS SPECTROMETRY: Mass=12011; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; CP000909; ABY35747.1; -; Genomic_DNA.
DR PIR; A55124; A55124.
DR RefSeq; WP_012258400.1; NC_010175.1.
DR RefSeq; YP_001636136.1; NC_010175.1.
DR AlphaFoldDB; Q7M1B9; -.
DR SMR; Q7M1B9; -.
DR STRING; 324602.Caur_2541; -.
DR EnsemblBacteria; ABY35747; ABY35747; Caur_2541.
DR KEGG; cau:Caur_2541; -.
DR PATRIC; fig|324602.8.peg.2864; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_0; -.
DR InParanoid; Q7M1B9; -.
DR OMA; QVGVAPK; -.
DR Proteomes; UP000002008; 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 Direct protein sequencing; Disulfide bond; Electron transport; Methylation;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..110
FT /note="Thioredoxin"
FT /id="PRO_0000120081"
FT DOMAIN 3..108
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOD_RES 105
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 105
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 32..35
FT /note="Redox-active"
FT VARIANT 42
FT /note="L -> N"
FT VARIANT 59
FT /note="N -> D"
FT VARIANT 60
FT /note="T -> V"
FT CONFLICT 18
FT /note="K -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..75
FT /note="IQGI -> LKGL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12131 MW; 279B37220146DBC8 CRC64;
MAKPIEVHDS DFAEKVLKSK TPVVVDFWAP WCGPCRVIAP ILDKLAGEYA GRLTIAKVNT
DDNVQYASQL GIQGIPTLVI FKDGREVGRL VGARPEAMYR EIFDKVLAMA
