ID F7ZI75_ROSLO Unreviewed; 534 AA.
AC F7ZI75;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|ARBA:ARBA00018719};
GN OrderedLocusNames=RLO149_c043150 {ECO:0000313|EMBL:AEI96211.1};
OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS 15278 / OCh 149).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI96211.1, ECO:0000313|Proteomes:UP000001353};
RN [1] {ECO:0000313|EMBL:AEI96211.1, ECO:0000313|Proteomes:UP000001353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC {ECO:0000313|Proteomes:UP000001353};
RX PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA Daniel R., Simon M., Brinkhoff T.;
RT "Comparative genome analysis and genome-guided physiological analysis of
RT Roseobacter litoralis.";
RL BMC Genomics 12:324-324(2011).
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DR EMBL; CP002623; AEI96211.1; -; Genomic_DNA.
DR RefSeq; WP_013964090.1; NC_015730.1.
DR AlphaFoldDB; F7ZI75; -.
DR STRING; 391595.RLO149_c043150; -.
DR KEGG; rli:RLO149_c043150; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_031864_5_8_5; -.
DR OrthoDB; 9786503at2; -.
DR Proteomes; UP000001353; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 12..131
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 534 AA; 57444 MW; 65AEA9B6432F5D5C CRC64;
MESLAPNIQE MTRTPLSEMH VEALRSAGEV VDFPADEVIF EVGDAMDKFT YIIEGGMEII
DPVTREAYLP TSLGPTQFVG EIAFLNGGAY SLPMRTTMAT KAIQVPREKM LELMSGLPEM
SDIIITVFAA RRRRQIEAGD TSLTLIGVDS DRNIRRIAEF ASRNKIPFKI QEPGSADAEA
KARVCGVPAD EPAVIFGSNR LVEDPTPEKV AELLGLVLDV KEDEVVDTLI VGGGPAGVAA
AVYAGAEGLS AIVVEDVAVG GQAGTSSRIE NYLGFPTGIS GADLVWRGEI QAMKFGTRFM
MPRRVENLER RPDGIFVAHL NNGQQLCAKS VVVATGVQYR RLPIERLEHF EGSGIYYAAT
EMEARYCKAS EAVIVGGGNS AGQAAMFLSR TARHVHVLIR GESLAASMSS YLSERLESTP
NITVHYKSQI TDLHGEADLG GLTINRNGEE WHLDTPAVFV MVGAAPNTGW LESHCALDPR
GFVLTGEDAA SPFETTCKGI FAVGDVRANS VKRVASSVGE GSVVISKVWE HVNS
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