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Database: UniProt
Entry: D3IG15_9BACT
LinkDB: D3IG15_9BACT
Original site: D3IG15_9BACT 
ID   D3IG15_9BACT            Unreviewed;       182 AA.
AC   D3IG15;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Antioxidant, AhpC/TSA family {ECO:0000313|EMBL:EFC68961.1};
DE            EC=1.11.1.15 {ECO:0000313|EMBL:EFC68961.1};
GN   ORFNames=HMPREF0670_00284 {ECO:0000313|EMBL:EFC68961.1};
OS   Prevotella sp. oral taxon 317 str. F0108.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575615 {ECO:0000313|EMBL:EFC68961.1, ECO:0000313|Proteomes:UP000003829};
RN   [1] {ECO:0000313|EMBL:EFC68961.1, ECO:0000313|Proteomes:UP000003829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0108 {ECO:0000313|EMBL:EFC68961.1,
RC   ECO:0000313|Proteomes:UP000003829};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., 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., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 317 strain F0108.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG740072; EFC68961.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3IG15; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_4_10; -.
DR   Proteomes; UP000003829; Unassembled WGS sequence.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EFC68961.1};
KW   Peroxidase {ECO:0000313|EMBL:EFC68961.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003829};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..182
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003045751"
FT   DOMAIN          43..182
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   182 AA;  20616 MW;  62255DE4FEAAAB7E CRC64;
     MNIKHLRRAT TALLVAFSLW SNTAKAQQST EVDYDAQYAS ELVKPGTVAP NFELPSPDGM
     KVSLSQFKGK YVVLDFWASW CPDCRKDAPN IVDLYNRFKD KGVAFVGISF DVDAALWKAA
     IEKYGMNYAH ASELKKMREA NISKTYGVKW IPSMVLVDPE GKVVMGTVLW KKLERKLEQL
     FR
//
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