ID A0A102DE97_9SPHN Unreviewed; 447 AA.
AC A0A102DE97;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|ARBA:ARBA00018719};
GN ORFNames=AQZ50_03400 {ECO:0000313|EMBL:KUR79926.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR79926.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR79926.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR79926.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUR79926.1}.
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DR EMBL; LLZR01000004; KUR79926.1; -; Genomic_DNA.
DR RefSeq; WP_067742697.1; NZ_KQ954286.1.
DR AlphaFoldDB; A0A102DE97; -.
DR STRING; 1739114.AQZ50_03400; -.
DR OrthoDB; 9779457at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR48105:SF33; OXIDOREDUCTASE; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT DOMAIN 51..81
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 82..111
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 447 AA; 46522 MW; C3F7C58D71AACB1A CRC64;
MIVTVALVPV YALPLLLAIG GWARHHALRT RRNRALLAHN RATGLAEPPS LHPVIDPARC
IGCGACVRAC PEHDVLGLVG RTATLIEPWA CVGHGTCRDA CPTGAIGLVF GTATRGIDLP
VLGPGSETSV AGLHIAGELG GLGLIRNAIN QGREAIDQIA AALARSPATA ADQLDLVIVG
CGPAGMAAGL GAIAHGLRFV ALDQATLGGS VAHYPRGKLV MTAPALLPLI GEVRLGSISK
EGLLAFWQDV LDRTGLSPRY EERVRDIERE DGGFVVVSNK ARYRARRVLL AMGRGGTPRR
LGVPGEDLAK VVYRLSDPGQ YAGLRVMIVG GGDSALEAAI ALAEFPETRI TLVHRGKAFD
RARRENRAAL GQTSGITQYL GARPVAITPD AAVIEDTSGT HAIPNDAIII CAGGTLPREW
LTQLGIAVET HRGLAPGAAD AAMAHSA
//