(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIJ4_GEOS0

ID   A0A0F6BIJ4_GEOS0        Unreviewed;       315 AA.
AC   A0A0F6BIJ4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 32.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881};
GN   OrderedLocusNames=GY4MC1_0404 {ECO:0000313|EMBL:ADP73245.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73245.1};
RN   [1] {ECO:0000313|EMBL:ADP73245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73245.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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:RU003881};
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; CP002293; ADP73245.1; -; Genomic_DNA.
DR   RefSeq; WP_003248086.1; NC_014650.1.
DR   EnsemblBacteria; ADP73245; ADP73245; GY4MC1_0404.
DR   GeneID; 29236938; -.
DR   KEGG; gmc:GY4MC1_0404; -.
DR   KO; K00384; -.
DR   OMA; VDNFPGY; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; GSP581103:G1GOQ-449-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 2.
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   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIJ4.
DR   SWISS-2DPAGE; A0A0F6BIJ4.
KW   FAD {ECO:0000256|RuleBase:RU003881};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003881};
KW   NADP {ECO:0000256|RuleBase:RU003881};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003881};
KW   Redox-active center {ECO:0000256|RuleBase:RU003881}.
FT   DOMAIN          7..294
FT                   /note="Pyr_redox_2"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   315 AA;  34406 MW;  F552612442376A09 CRC64;
     MSEEKIYDVI IAGAGPAGMT AAVYTSRANL STLMIERGVP GGQMVNTEEV ENYPGYEQIL
     GPELATKMFE HAKKFGAEYA YGEVKEIIDG EAYKTVVVGD KQYKGRAVII ATGAEYKKLG
     VPGEAEYGGR GVSYCAVCDG AFFKGKDLVV VGGGDSAVEE GVYLTRFANK VTIVHRRDQL
     RAQKILQDRA FANEKIDFIW NHTVKQINGK DGKVNSVTLV HTQTGEEREF PCDGVFIYIG
     MLPLSKPFVN LGITNENGYI VTNERMETKV PGIFAAGDVR EKSLRQIVTA TGDGSIAAQS
     AQHYVEELKE KLNIK
//

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