ID D0KVY5_HALNC Unreviewed; 319 AA.
AC D0KVY5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN OrderedLocusNames=Hneap_0046 {ECO:0000313|EMBL:ACX94912.1};
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX94912.1, ECO:0000313|Proteomes:UP000009102};
RN [1] {ECO:0000313|EMBL:ACX94912.1, ECO:0000313|Proteomes:UP000009102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) 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|ARBA:ARBA00009333,
CC ECO:0000256|RuleBase:RU003880}.
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DR EMBL; CP001801; ACX94912.1; -; Genomic_DNA.
DR RefSeq; WP_012822949.1; NC_013422.1.
DR AlphaFoldDB; D0KVY5; -.
DR STRING; 555778.Hneap_0046; -.
DR KEGG; hna:Hneap_0046; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_6; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000009102; 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 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 NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009102}.
FT DOMAIN 10..303
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 319 AA; 33899 MW; AC8AE3A0F5F4FB71 CRC64;
MSETNTRHAR LLILGSGPAG YAAAVYAARA NLNPVLITGM EMGGQLTTTT EVENWPGDPG
DLTGPALMDR MKAHAEKFDT EIIFDHIQST NLKQRPFTLK GDSGTYTCDA LIVATGASAK
YLGLESESKF KGKGVSACAT CDGFFYKNQE IAVVGGGNTA VEEALYLANV ASKVHVIHRR
DKFKAENILI DRLMKKVDEG KVEIHWHSAI DEILGDNTGV TGLRIKQVQT EKTTDIALTG
VFIAIGHAPN TGIFEGELDL AGGYIQVKSG TQGNATATSV PGVFAAGDVM DHVYRQAITS
AGTGCMAALD AKTYLEGLE
//
