ID F9Z5H6_ODOSD Unreviewed; 333 AA.
AC F9Z5H6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ADY31547.1};
GN OrderedLocusNames=Odosp_0458 {ECO:0000313|EMBL:ADY31547.1};
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:ADY31547.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY31547.1, 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; ADY31547.1; -; Genomic_DNA.
DR AlphaFoldDB; F9Z5H6; -.
DR STRING; 709991.Odosp_0458; -.
DR PaxDb; 709991-Odosp_0458; -.
DR KEGG; osp:Odosp_0458; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_1_0_10; -.
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; IPR025380; DUF4369.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
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 Pfam; PF14289; DUF4369; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006657}.
FT DOMAIN 192..333
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 333 AA; 37758 MW; 8F97C3FB371F66E9 CRC64;
MVCIISYLDK KADTLAKAEI KEEKFELKGK VSNLTIATLQ IPGKGIGHAP IYLENTDYTV
RLNPQNLEMS EIIGGGESQK IAHGLFLIDQ NLSQAIDSIR DEYIKEANNP QSTRFQELNT
FLDSIQQTIE KQKEAFLQKN ATTYVALNHI AQNADRMNLK ELTERYELFP AELQNSLLGQ
QIKTQIKKMQ TLAPGQIAPD FTVQTPDGKS FNLHSIKAKA KIIDFWASWC APCRALTPQL
VKLYNEFHEQ GLEIIGISLD DKKEAWIKAI EEENIPWFQG SKLDGFKPDN PLNQLYGIHG
IPHIVLLNTD NQIVVTTTDI KILREEILKL FKQ
//
