THIO_PSEAE
ID THIO_PSEAE Reviewed; 108 AA.
AC Q9X2T1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; Synonyms=trx; OrderedLocusNames=PA5240;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8830;
RX PubMed=10224002; DOI=10.1128/aem.65.5.2065-2071.1999;
RA Zago A., Chugani S., Chakrabarty A.M.;
RT "Cloning and characterization of polyphosphate kinase and
RT exopolyphosphatase genes from Pseudomonas aeruginosa 8830.";
RL Appl. Environ. Microbiol. 65:2065-2071(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AF053463; AAD29108.2; -; Genomic_DNA.
DR EMBL; AE004091; AAG08625.1; -; Genomic_DNA.
DR PIR; G82991; G82991.
DR RefSeq; NP_253927.1; NC_002516.2.
DR RefSeq; WP_003096336.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9X2T1; -.
DR SMR; Q9X2T1; -.
DR STRING; 287.DR97_2610; -.
DR PaxDb; Q9X2T1; -.
DR PRIDE; Q9X2T1; -.
DR DNASU; 877946; -.
DR EnsemblBacteria; AAG08625; AAG08625; PA5240.
DR GeneID; 877946; -.
DR KEGG; pae:PA5240; -.
DR PATRIC; fig|208964.12.peg.5492; -.
DR PseudoCAP; PA5240; -.
DR HOGENOM; CLU_090389_10_2_6; -.
DR InParanoid; Q9X2T1; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; Q9X2T1; -.
DR BioCyc; PAER208964:G1FZ6-5360-MON; -.
DR Proteomes; UP000002438; 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 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..108
FT /note="Thioredoxin"
FT /id="PRO_0000120120"
FT DOMAIN 2..108
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"
SQ SEQUENCE 108 AA; 11870 MW; 908A6E87385C6AD8 CRC64;
MSEHIVNVTD ASFEQDVLKA DGPVLVDYWA EWCGPCKMIA PVLDEVARDY QGKLKVCKLN
IDENQDTPPK YGVRGIPTLM LFKDGNVEAT KVGALSKSQL AAFLDANI