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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//