ID Q46HG2_PROMT Unreviewed; 318 AA.
AC Q46HG2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Thioredoxin-disulfide reductase {ECO:0000313|EMBL:AAZ59066.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:AAZ59066.1};
GN OrderedLocusNames=PMN2A_1578 {ECO:0000313|EMBL:AAZ59066.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ59066.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ59066.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ59066.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000095; AAZ59066.1; -; Genomic_DNA.
DR RefSeq; WP_011294211.1; NC_007335.2.
DR AlphaFoldDB; Q46HG2; -.
DR STRING; 59920.PMN2A_1578; -.
DR KEGG; pmn:PMN2A_1578; -.
DR HOGENOM; CLU_031864_5_1_3; -.
DR OrthoDB; 9806179at2; -.
DR PhylomeDB; Q46HG2; -.
DR Proteomes; UP000002535; Chromosome.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAZ59066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002535}.
FT DOMAIN 7..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 318 AA; 34402 MW; 299E1E3DC0CFFABD CRC64;
METIETDVVI VGGGPAGCSC ALYTSRADLR TVILDKNPDV GALAITHQIA NYPGVSSEMS
GEALLKLMRD QATQYGADYR RAQVFGIDSS GDWKTIYTPE GTFKAKALVV ASGAMGRPAS
FKGEAEFLGR GVSYCATCDG AFYRDREVAV VGINKEAIEE ANVLTKFASK VHWITSNDPK
PDDHHAQDLL SKPNVNHWSK TRLMQIEGND GGVTGIKVKN RSIDTHQNLA LEGVFVYMSG
SKPITDFLGE QVAFKEDGGV LVDDFMSTTV EGVWAIGDIR NTPFKQAVVA ASDGCIAAMA
IDRYLNSRKS IRVDWVHA
//
