(data stored in ACNUC7421 zone)

SWISSPROT: D6Z9I0_SEGRD

ID   D6Z9I0_SEGRD            Unreviewed;       323 AA.
AC   D6Z9I0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881};
GN   OrderedLocusNames=Srot_0014 {ECO:0000313|EMBL:ADG96507.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96507.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96507.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide
CC         + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698,
CC         Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.8.1.9; 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; CP001958; ADG96507.1; -; Genomic_DNA.
DR   RefSeq; WP_013136963.1; NC_014168.1.
DR   STRING; 640132.Srot_0014; -.
DR   EnsemblBacteria; ADG96507; ADG96507; Srot_0014.
DR   KEGG; srt:Srot_0014; -.
DR   eggNOG; ENOG4105C3M; Bacteria.
DR   eggNOG; COG0492; LUCA.
DR   HOGENOM; HOG000072912; -.
DR   KO; K00384; -.
DR   OMA; GFMANGF; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; SROT640132:G1GLH-16-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
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; D6Z9I0.
DR   SWISS-2DPAGE; D6Z9I0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN        7    294       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
SQ   SEQUENCE   323 AA;  34213 MW;  BBB2DE6DD17A4E5A CRC64;
     MPETLENLII IGSGPAGYTA AVYAARAQLN PLVFEGTQFG GSLMTTTEVE NFPGFQEGVQ
     GPDLMVEMRS QAERFGARLQ TKDVEWVELG GDRKLVHVDG EVHAARAVIL AMGAAPRYLG
     VPGEQELLGR GVSSCATCDG FFFKDQDIAV IGGGDSAMEE ATFLTRFAKS VTLIHRRDEF
     RASRIMLERA KSNPKIKFVL GASVSRVLGS TSVTGVELSH VATGQTSELP VTGLFVAIGH
     DPRAELVVGQ VDQDEDGYVK VQAPSSATST PGVFAAGDLV DRHYRQAITA AGSGCVAAID
     AERWLAAAET AQAAPRHALS AQH
//

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