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Database: UniProt
Entry: E2S5Z5_9CORY
LinkDB: E2S5Z5_9CORY
Original site: E2S5Z5_9CORY 
ID   E2S5Z5_9CORY            Unreviewed;       302 AA.
AC   E2S5Z5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFQ79437.1};
GN   ORFNames=HMPREF0305_11947 {ECO:0000313|EMBL:EFQ79437.1};
OS   Corynebacterium pseudogenitalium ATCC 33035.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=525264 {ECO:0000313|EMBL:EFQ79437.1, ECO:0000313|Proteomes:UP000003020};
RN   [1] {ECO:0000313|EMBL:EFQ79437.1, ECO:0000313|Proteomes:UP000003020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33035 {ECO:0000313|EMBL:EFQ79437.1,
RC   ECO:0000313|Proteomes:UP000003020};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2010) 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};
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:EFQ79437.1}.
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DR   EMBL; ABYQ02000014; EFQ79437.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2S5Z5; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_0_11; -.
DR   OrthoDB; 9786503at2; -.
DR   Proteomes; UP000003020; 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; 2.
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          4..150
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          184..283
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   302 AA;  32118 MW;  4904DCB0AD669900 CRC64;
     MYPDVIIIGG GFAGTAAAIT LARANRNIQL IDSGAPRNRF SEHAHGILGL DGAAPAELLQ
     RGHAEVKKFG GTITHGSVEK LTRTSEHEPW QAKLASGEVL ESRHVLIATG LTDKLPAVPG
     LRDLWGTRVF HCPYCHGYEV TGKKVALIGG ANPPFTIRIS KLLSTWTDTL TFYPNGLELT
     DLDRAQLAGL GVEVNDAQVT QVRPEEASST GVVVQSSTGE DTYEACFTGP DFLPNDALLR
     DAGCESTYGW VSVERGQTSV PRLWAAGNVV SSPDQVSQAM GSGAAVGIAI DQRMLDEDLA
     EL
//
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