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 16-JUN-2009, entry version 66. DE RecName: Full=Thioredoxin; DE Short=Trx; GN Name=trxA; OrderedLocusNames=slr0623; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96347399; PubMed=8756494; DOI=10.1104/pp.111.4.1067; RA Navarro F., Florencio F.J.; RT "The cyanobacterial thioredoxin gene is required for both RT photoautotrophic and heterotrophic growth."; RL Plant Physiol. 111:1067-1075(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=96127529; 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 RT region 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]. RX MEDLINE=97061201; 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., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [4] RP PROTEIN SEQUENCE OF 2-18. RX MEDLINE=97443974; 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 CC system. Participates in various redox reactions through the CC reversible oxidation of its active center dithiol to a disulfide CC and catalyzes dithiol-disulfide exchange reactions. CC -!- INTERACTION: CC P73829:-; NbExp=1; IntAct=EBI-862916, EBI-865957; CC P74729:-; NbExp=1; IntAct=EBI-862916, EBI-862735; CC Q01950:apcC; NbExp=1; IntAct=EBI-862916, EBI-862779; CC Q55544:apcE; NbExp=1; IntAct=EBI-862916, EBI-862826; CC P77973:argG; NbExp=1; IntAct=EBI-862916, EBI-862317; CC P54205:cbbL; NbExp=1; IntAct=EBI-862916, EBI-862277; CC P72758:ccmM; NbExp=1; IntAct=EBI-862916, EBI-862848; CC P28371:fusA; NbExp=1; IntAct=EBI-862916, EBI-862177; CC P72623:glgA2; NbExp=1; IntAct=EBI-862916, EBI-862297; CC P52981:glgB; NbExp=1; IntAct=EBI-862916, EBI-862111; CC P52415:glgC; NbExp=1; IntAct=EBI-862916, EBI-865829; CC P55037:gltB; NbExp=2; IntAct=EBI-862916, EBI-862093; CC P55038:gltS; NbExp=1; IntAct=EBI-862916, EBI-862080; CC Q05972:groL1; NbExp=1; IntAct=EBI-862916, EBI-862119; CC P77969:hemB; NbExp=1; IntAct=EBI-862916, EBI-862729; CC P74643:pgm; NbExp=1; IntAct=EBI-862916, EBI-862197; CC P72586:rfbD; NbExp=1; IntAct=EBI-862916, EBI-862716; CC P77965:rpoB; NbExp=1; IntAct=EBI-862916, EBI-862811; CC P73334:rpoC2; NbExp=1; IntAct=EBI-862916, EBI-862802; CC P73314:rpsC; NbExp=1; IntAct=EBI-862916, EBI-862866; CC P74241:sat; NbExp=1; IntAct=EBI-862916, EBI-862859; CC P72854:sir; NbExp=1; IntAct=EBI-862916, EBI-862835; CC P73728:sll1621; NbExp=1; IntAct=EBI-862916, EBI-862771; CC P74227:tuf; NbExp=1; IntAct=EBI-862916, EBI-862703; CC Q55522:valS; NbExp=1; IntAct=EBI-862916, EBI-862103; CC -!- SIMILARITY: Belongs to the thioredoxin family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80486; CAA56653.1; -; Genomic_DNA. DR EMBL; BA000022; BAA10623.1; -; Genomic_DNA. DR PIR; S46958; S46958. DR RefSeq; NP_442553.1; -. DR HSSP; P23400; 1DBY. DR IntAct; P52231; 80. DR GeneID; 952277; -. DR GenomeReviews; BA000022_GR; slr0623. DR KEGG; syn:slr0623; -. DR NMPDR; fig|1148.1.peg.2654; -. DR HOGENOM; P52231; -. DR OMA; P52231; MNVDENR. DR BioCyc; SSP1148:SLR0623-MON; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR017936; Thioredoxin-like. DR InterPro; IPR006662; Thioredoxin-like_subdom. DR InterPro; IPR015467; Thioredoxin_core. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR PANTHER; PTHR10438; Trx; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Electron transport; Redox-active center; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 107 Thioredoxin. FT /FTId=PRO_0000120138. FT DOMAIN 2 107 Thioredoxin. FT DISULFID 32 35 Redox-active (By similarity). SQ SEQUENCE 107 AA; 11749 MW; C03FAA09EACEC333 CRC64; MSATPQVSDA SFKEDVLDSE LPVLVDFWAP WCGPCRMVAP VVDEISQQYE GKVKVVKLNT DENPNTASQY GIRSIPTLMI FKGGQRVDMV VGAVPKTTLA STLEKYL //