ID F9ZAK0_ODOSD Unreviewed; 291 AA.
AC F9ZAK0;
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=Redoxin domain protein {ECO:0000313|EMBL:ADY33291.1};
GN OrderedLocusNames=Odosp_2295 {ECO:0000313|EMBL:ADY33291.1};
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:ADY33291.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY33291.1, 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; ADY33291.1; -; Genomic_DNA.
DR RefSeq; WP_013612484.1; NZ_CP086000.1.
DR AlphaFoldDB; F9ZAK0; -.
DR STRING; 709991.Odosp_2295; -.
DR PaxDb; 709991-Odosp_2295; -.
DR GeneID; 69855313; -.
DR KEGG; osp:Odosp_2295; -.
DR eggNOG; COG0526; Bacteria.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_955924_0_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; 2.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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 Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006657};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..291
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003392336"
FT DOMAIN 14..135
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 151..290
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 291 AA; 32925 MW; 1B8D52744EC92313 CRC64;
MKQVYFIIAM LCGLALGGQA QGIRFAEGSW KELLETAKKE GKLIFVDCYT EWCQPCKQME
QQVFPSEKVG KFYNEHFINV KMDMEKGEGP VILNTYKINA FPTLLFVNGE GGEVYRIVGS
KKEAELLQVG ADALASKTVY PVNSQAQQQI ALIGREIPDF CYRDSTGKEV KFSSFRGNYV
YVDMWATWCR PCCEEIPYMG ELEKKFHGKK ICFVSLSCDK DLQAWKKKLR TDRMGGIQLN
CGGDPAFMKF FGIQGIPHFI LLDPEGKVVN PNMSRPSQEI TVETLSRLKG I
//
