ID   Q819J1_BACCR            Unreviewed;        78 AA.
AC   Q819J1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=NRDH-redoxin {ECO:0000313|EMBL:AAP10907.1};
GN   OrderedLocusNames=BC_3987 {ECO:0000313|EMBL:AAP10907.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10907.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP10907.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2] {ECO:0007829|PDB:3ZIJ, ECO:0007829|PDB:3ZIT}
RP   X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=23936007; DOI=10.1371/JOURNAL.PONE.0069411;
RA   Rohr A.K., Hammerstad M., Andersson K.K.;
RT   "Tuning of thioredoxin redox properties by intramolecular hydrogen bonds.";
RL   PLoS ONE 8:e69411-e69411(2013).
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DR   EMBL; AE016877; AAP10907.1; -; Genomic_DNA.
DR   RefSeq; NP_833706.1; NC_004722.1.
DR   RefSeq; WP_000717875.1; NZ_CP034551.1.
DR   PDB; 3ZIJ; X-ray; 1.40 A; A/B=1-78.
DR   PDB; 3ZIT; X-ray; 1.18 A; A/B=1-78.
DR   PDBsum; 3ZIJ; -.
DR   PDBsum; 3ZIT; -.
DR   AlphaFoldDB; Q819J1; -.
DR   SMR; Q819J1; -.
DR   GeneID; 67468300; -.
DR   KEGG; bce:BC3987; -.
DR   PATRIC; fig|226900.8.peg.4114; -.
DR   HOGENOM; CLU_026126_9_3_9; -.
DR   OrthoDB; 9795531at2; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   CDD; cd02976; NrdH; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011911; GlrX_YruB.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02196; GlrX_YruB; 1.
DR   PANTHER; PTHR34386; GLUTAREDOXIN; 1.
DR   PANTHER; PTHR34386:SF1; GLUTAREDOXIN-LIKE PROTEIN NRDH; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3ZIJ, ECO:0007829|PDB:3ZIT};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT   DOMAIN          4..63
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   DISULFID        12..15
FT                   /evidence="ECO:0007829|PDB:3ZIJ, ECO:0007829|PDB:3ZIT"
SQ   SEQUENCE   78 AA;  8995 MW;  0EDA3E97229BB2AC CRC64;
     MKKIEVYTQP DCPPCVIVKE FLKHNNVAYE EFDVKKDAAA RNRLLYDYDS YSTPTVVIDG
     EVVAGFQIEK LQQLLNIE
//