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Database: UniProt
Entry: R6XVI7_9BACT
LinkDB: R6XVI7_9BACT
Original site: R6XVI7_9BACT 
ID   R6XVI7_9BACT            Unreviewed;       276 AA.
AC   R6XVI7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Alkyl hydroperoxide reductase/Thiol specific antioxidant/Mal allergen {ECO:0000313|EMBL:CDD20316.1};
GN   ORFNames=BN769_00432 {ECO:0000313|EMBL:CDD20316.1};
OS   Prevotella sp. CAG:732.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262934 {ECO:0000313|EMBL:CDD20316.1, ECO:0000313|Proteomes:UP000018039};
RN   [1] {ECO:0000313|EMBL:CDD20316.1, ECO:0000313|Proteomes:UP000018039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:732 {ECO:0000313|Proteomes:UP000018039};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDD20316.1}.
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DR   EMBL; CBGP010000124; CDD20316.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6XVI7; -.
DR   Proteomes; UP000018039; Unassembled WGS sequence.
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; IPR013740; Redoxin.
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; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018039};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..276
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004424720"
FT   DOMAIN          133..276
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   276 AA;  31658 MW;  E548F5B852E32898 CRC64;
     MKQLKNYMML LLLVPCFCMA QGCKPASTKP MVTSDHYNQD SLEEVVAAAM PQMEYKDEMS
     MLKAYFKAID QKVTPKEWAD RMKADAIASI FDCFCTSDMK EVYSFFLDNC QVDSLREKVK
     SHYEAMTNKY GHLFPGKPAP NLTFTDKNGK QLSLQSFKGQ VLLVDIWGTW CAPCIAEMPY
     LAALQKEYGS RKDVRIMSIA CDKKAEKWKT YLASHPTTWH QYLITGEGNQ TLDKAYFCEG
     IPRFIIIDKQ GNIVAADAMR PSEKDFREYF RKIVNP
//
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