ID A0A076H8Y8_9SYNE Unreviewed; 460 AA.
AC A0A076H8Y8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=KR49_05115 {ECO:0000313|EMBL:AII45836.1};
OS Synechococcus sp. KORDI-49.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585423 {ECO:0000313|EMBL:AII45836.1, ECO:0000313|Proteomes:UP000028589};
RN [1] {ECO:0000313|EMBL:AII45836.1, ECO:0000313|Proteomes:UP000028589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-49 {ECO:0000313|EMBL:AII45836.1,
RC ECO:0000313|Proteomes:UP000028589};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequences of Synechococcus sp. KORDI-49.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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DR EMBL; CP006270; AII45836.1; -; Genomic_DNA.
DR RefSeq; WP_043692170.1; NZ_CP006270.1.
DR AlphaFoldDB; A0A076H8Y8; -.
DR STRING; 585423.KR49_05115; -.
DR KEGG; synr:KR49_05115; -.
DR PATRIC; fig|585423.3.peg.982; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_4_3; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000028589; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF26; NADPH-DEPENDENT THIOREDOXIN REDUCTASE 3; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003880}.
FT DOMAIN 331..458
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 460 AA; 49363 MW; 1AE87E0EB6C9A54A CRC64;
MAAGSASETV ENLVIVGSGP AGYTAAIYAA RANLQPLLIT GFQRGGIPGG QLMTTTDVEN
FPGFPDGVLG PDLMDLMRAQ AVRWGTHLLE ADADEIDLSQ RPFRIKADGR TLLTHALVIA
TGASANRLGL PSEERFWSSG ISACAICDGA TPQFRNAELA VVGGGDSACE EAVYLTKYGS
HVHQIVRSEQ LRASAAMADR VRANPAITLH WNSEVVDVSG NGWMESLTLR DRSTGDQASL
AAKGLFYAIG HTPNTDLLKE QLSLDAKGYV ITEPGRPETS IEGVFAAGDV ADAEWRQGIT
AAGSGCKAAL AAERWLTHHD LAQRVQRRSV DPAKAEMPVN VAVTTEETYA PDAPWQKGSY
ALRKLYHDSS RPLLVIYTSP SCGPCHVLKP QLKRVITELE GRAQAVVIDI EADQDIAEQA
GVNGTPTVQL FHRKSMVEQW RGVKQRSTFK SAIEALLEPA
//
