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Database: UniProt
Entry: F3NTR2_9ACTN
LinkDB: F3NTR2_9ACTN
Original site: F3NTR2_9ACTN 
ID   F3NTR2_9ACTN            Unreviewed;       346 AA.
AC   F3NTR2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:EGG43222.1};
GN   ORFNames=SGM_6362 {ECO:0000313|EMBL:EGG43222.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG43222.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG43222.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG43222.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
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|ARBA:ARBA00000849};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EGG43222.1}.
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DR   EMBL; AEYX01000046; EGG43222.1; -; Genomic_DNA.
DR   RefSeq; WP_006144246.1; NZ_AEYX01000046.1.
DR   AlphaFoldDB; F3NTR2; -.
DR   STRING; 996637.SGM_6362; -.
DR   eggNOG; COG0492; Bacteria.
DR   Proteomes; UP000003022; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 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   Reference proteome {ECO:0000313|Proteomes:UP000003022}.
FT   DOMAIN          15..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   346 AA;  36063 MW;  4CB722431A1EA501 CRC64;
     MTETQRTHDT HPDRYEVLVV GGGAAGLSAG LVLGRARRRT LVVDAGEPRN APAAHMQGYL
     SRDGMPPAEL LAAGRAEIAR YGTVELVTDR VVDLARDGAE GGAPLGFTAH LAGGRTVRAR
     RVLVATGLKD ELPPVPGVAE RWGRDVLHCP YCHGWEVRDE AFGVLATSPM SVHQALLVSH
     WSKDTTLFLN GVAEADLSDE ELRRLAAAGV DVVPGGVAGL VVEDDRITGV RLADGSVHAR
     SVVFVASRMV PRTGLLEKLG AELRETPVGA CPVVDETGRT TVPGVWAAGN ATLVAQQVVN
     AASTGYTAAA AVNAELVFED IDARVGVTRT GGTGRTAEAA EAAAEV
//
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