ID D6M2V2_STRSH Unreviewed; 315 AA.
AC D6M2V2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein {ECO:0000313|EMBL:EFG64940.2};
DE Flags: Fragment;
GN ORFNames=SSBG_05742 {ECO:0000313|EMBL:EFG64940.2};
OS Streptomyces sp. (strain SPB074).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EFG64940.2, ECO:0000313|Proteomes:UP000002779};
RN [1] {ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFG64940.2, ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain SPB74.";
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|ARBA:ARBA00000849};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; GG770539; EFG64940.2; -; Genomic_DNA.
DR AlphaFoldDB; D6M2V2; -.
DR Proteomes; UP000002779; 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}.
FT DOMAIN 37..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT NON_TER 315
FT /evidence="ECO:0000313|EMBL:EFG64940.2"
SQ SEQUENCE 315 AA; 32987 MW; AF763D8C01B26CE9 CRC64;
MLCRNGKDVC LSRRVCRTVA ATQGEVVVAM TEVRERYDAV VVGGGPAGLA GALTLARARR
SVLVLDAGEP RNAPAEGAHG VLGLEGIEPA ELLRRGRAEV RGYGGEVVAG EVVDVRRDRD
GFAVTSADGA VVRARAVLVA SGLVDGLPEV PGLRAHWGGD VVHCPYCHGW EVRERAIGVL
GTGPMSLHQV KLFRQWSDDL VYFPDRQPVP DDEWIAARGI RVVPGEVAGV ESDAEGRLAG
VRMADGTFVP RRALAVATRM EARAGFLAGL GLTPVPHPSG MGTHIPAEPT GRTTVPGLWI
AGNATDLSAQ VGASA
//
