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Database: UniProt
Entry: Q6NGT3_CORDI
LinkDB: Q6NGT3_CORDI
Original site: Q6NGT3_CORDI 
ID   Q6NGT3_CORDI            Unreviewed;       198 AA.
AC   Q6NGT3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Iron repressible polypeptide (Putative reductase) {ECO:0000313|EMBL:CAE49951.1};
GN   Name=dirA {ECO:0000313|EMBL:CAE49951.1};
GN   OrderedLocusNames=DIP1420 {ECO:0000313|EMBL:CAE49951.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49951.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE49951.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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DR   EMBL; BX248358; CAE49951.1; -; Genomic_DNA.
DR   RefSeq; WP_003851816.1; NC_002935.2.
DR   AlphaFoldDB; Q6NGT3; -.
DR   STRING; 257309.DIP1420; -.
DR   GeneID; 83708002; -.
DR   KEGG; cdi:DIP1420; -.
DR   HOGENOM; CLU_042529_21_3_11; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198}.
FT   DOMAIN          4..170
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        61
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   198 AA;  22365 MW;  7A09C8F1B43205DD CRC64;
     MSILTVGEKF PEFNLTALKG GDLHDVNASQ PEDYFETVSL DKYEGKWKVV FFYPKDFTFV
     CPTEIAAFGK LDEEFQDRDT QILGGSIDNE FSHFNWRATH PELKTVPFPL FSDIKHDLIK
     ALGVENEEGV ADRATFIIDP DGIIQFVSVT PDAVGRNVDE VLRVLDALQS EEVCACNWQK
     NDPTKNIDKF AELEKGLN
//
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