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Thioredoxin reductase (EC 1.8.1.9)

 I9T3T7_HELPX            Unreviewed;       311 AA.
I9T3T7;
03-OCT-2012, integrated into UniProtKB/TrEMBL.
03-OCT-2012, sequence version 1.
25-APR-2018, entry version 36.
RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881};
EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881};
Name=trxB {ECO:0000313|EMBL:EJB64991.1};
ORFNames=HPHPH43_0867 {ECO:0000313|EMBL:EJB64991.1};
Helicobacter pylori Hp H-43.
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Helicobacteraceae; Helicobacter.
NCBI_TaxID=992048 {ECO:0000313|EMBL:EJB64991.1, ECO:0000313|Proteomes:UP000004515};
[1] {ECO:0000313|EMBL:EJB64991.1, ECO:0000313|Proteomes:UP000004515}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hp H-43 {ECO:0000313|EMBL:EJB64991.1,
ECO:0000313|Proteomes:UP000004515};
PubMed=23661595; DOI=10.1111/2049-632X.12045;
Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
"Genome sequences of 65 Helicobacter pylori strains isolated from
asymptomatic individuals and patients with gastric cancer, peptic
ulcer disease, or gastritis.";
Pathog. Dis. 68:39-43(2013).
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH. {ECO:0000256|RuleBase:RU003881}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|RuleBase:RU003881};
Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
-!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJB64991.1}.
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EMBL; AKOO01000004; EJB64991.1; -; Genomic_DNA.
RefSeq; WP_000564430.1; NZ_AKOO01000004.1.
ProteinModelPortal; I9T3T7; -.
EnsemblBacteria; EJB64991; EJB64991; HPHPH43_0867.
PATRIC; fig|992048.3.peg.850; -.
OrthoDB; POG091H02HU; -.
Proteomes; UP000004515; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
InterPro; IPR005982; Thioredox_Rdtase.
Pfam; PF07992; Pyr_redox_2; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 1.
TIGRFAMs; TIGR01292; TRX_reduct; 1.
PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000004515};
FAD {ECO:0000256|RuleBase:RU003880};
Flavoprotein {ECO:0000256|RuleBase:RU003880};
NADP {ECO:0000256|RuleBase:RU003881};
Oxidoreductase {ECO:0000256|RuleBase:RU003880,
ECO:0000256|SAAS:SAAS00270604, ECO:0000313|EMBL:EJB64991.1};
Redox-active center {ECO:0000256|RuleBase:RU003880}.
DOMAIN 3 297 FAD/NAD-binding_dom.
{ECO:0000259|Pfam:PF07992}.
SEQUENCE 311 AA; 33511 MW; F9E900FA4B3A51F7 CRC64;
MIDCAIIGGG PAGLSAGLYA TRGGVKNAVL FEKGMPGGQI TGSSEIENYP GVKEVVSGLD
FMQPWQEQCF RFGLKHEMTA VQRVSKKDSH FVILAEDGKT FEAKSVIIAT GGSPKRTGIK
GESEYWGKGV STCATCDGFF YKNKEVAVLG GGDTAVEEAI YLANICKKVY LIHRRDGFRC
APITLEHAKN NDKIEFLTPY VVEEIKGDAS GVSSLSIKNT ATNETRELVV PGFFIFVGYD
VNNAVLKQED NSMLCKCDEY GSIVVDFSMK TNVQGLFAAG DIRIFAPKQV VCAASDGATA
ALSVISYLEH H


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