THIO_SYNY3
ID THIO_SYNY3 Reviewed; 107 AA.
AC P52231;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=slr0623;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8756494; DOI=10.1104/pp.111.4.1067;
RA Navarro F., Florencio F.J.;
RT "The cyanobacterial thioredoxin gene is required for both photoautotrophic
RT and heterotrophic growth.";
RL Plant Physiol. 111:1067-1075(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
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.
CC -!- INTERACTION:
CC P52231; Q55544: apcE; NbExp=4; IntAct=EBI-862916, EBI-862826;
CC P52231; P77973: argG; NbExp=2; IntAct=EBI-862916, EBI-862317;
CC P52231; P54205: cbbL; NbExp=3; IntAct=EBI-862916, EBI-862277;
CC P52231; P72758: ccmM; NbExp=2; IntAct=EBI-862916, EBI-862848;
CC P52231; P28371: fusA; NbExp=2; IntAct=EBI-862916, EBI-862177;
CC P52231; P55037: gltB; NbExp=2; IntAct=EBI-862916, EBI-862093;
CC P52231; Q05972: groEL1; NbExp=4; IntAct=EBI-862916, EBI-862119;
CC P52231; P74643: pgm; NbExp=2; IntAct=EBI-862916, EBI-862197;
CC P52231; P72586: rfbD; NbExp=2; IntAct=EBI-862916, EBI-862716;
CC P52231; P73314: rpsC; NbExp=5; IntAct=EBI-862916, EBI-862866;
CC P52231; P72854: sir; NbExp=3; IntAct=EBI-862916, EBI-862835;
CC P52231; P73728: sll1621; NbExp=3; IntAct=EBI-862916, EBI-862771;
CC P52231; P73348: slr1198; NbExp=4; IntAct=EBI-862916, EBI-862753;
CC P52231; P74227: tuf; NbExp=5; IntAct=EBI-862916, EBI-862703;
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; X80486; CAA56653.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10623.1; -; Genomic_DNA.
DR PIR; S46958; S46958.
DR AlphaFoldDB; P52231; -.
DR SMR; P52231; -.
DR IntAct; P52231; 103.
DR STRING; 1148.1208455; -.
DR PaxDb; P52231; -.
DR EnsemblBacteria; BAA10623; BAA10623; BAA10623.
DR KEGG; syn:slr0623; -.
DR eggNOG; COG3118; Bacteria.
DR InParanoid; P52231; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P52231; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..107
FT /note="Thioredoxin"
FT /id="PRO_0000120138"
FT DOMAIN 2..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 107 AA; 11749 MW; C03FAA09EACEC333 CRC64;
MSATPQVSDA SFKEDVLDSE LPVLVDFWAP WCGPCRMVAP VVDEISQQYE GKVKVVKLNT
DENPNTASQY GIRSIPTLMI FKGGQRVDMV VGAVPKTTLA STLEKYL
