ID F9Z334_ODOSD Unreviewed; 168 AA.
AC F9Z334;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ADY32418.1};
GN OrderedLocusNames=Odosp_1379 {ECO:0000313|EMBL:ADY32418.1};
OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY32418.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY32418.1, ECO:0000313|Proteomes:UP000006657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC {ECO:0000313|Proteomes:UP000006657};
RX PubMed=21677857; DOI=10.4056/sigs.1714269;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Odoribacter splanchnicus type strain
RT (1651/6).";
RL Stand. Genomic Sci. 4:200-209(2011).
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DR EMBL; CP002544; ADY32418.1; -; Genomic_DNA.
DR RefSeq; WP_013611626.1; NZ_CP086000.1.
DR AlphaFoldDB; F9Z334; -.
DR STRING; 709991.Odosp_1379; -.
DR PaxDb; 709991-Odosp_1379; -.
DR GeneID; 69856251; -.
DR KEGG; osp:Odosp_1379; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_11_2_10; -.
DR OrthoDB; 9794348at2; -.
DR BioCyc; OSPL709991:G1GRN-1394-MONOMER; -.
DR Proteomes; UP000006657; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000006657};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..168
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003392126"
FT DOMAIN 32..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 168 AA; 19221 MW; 236BF9635DC58697 CRC64;
MKNTIILLTM LLFSGIGFAQ ESNNGKQLWA KSFLNEKAPE LTVETWISKK PDTEGKFVII
DFWATWCGPC RKAIPELNEI AKEFSKDVVV IGISDEPVEK IKAMKEPVIE YYYGVDTKKT
MDKILEIKGI PHVIIIDPKG IVRWEGFPLL ENHKLTPEVV KNLIEKYK
//
