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Database: UniProt
Entry: A0A0F2NXC1_9FLAO
LinkDB: A0A0F2NXC1_9FLAO
Original site: A0A0F2NXC1_9FLAO 
ID   A0A0F2NXC1_9FLAO        Unreviewed;       177 AA.
AC   A0A0F2NXC1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:KJS04922.1};
GN   ORFNames=VR77_10290 {ECO:0000313|EMBL:KJS04922.1};
OS   Flavobacteriales bacterium BRH_c54.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS04922.1, ECO:0000313|Proteomes:UP000033681};
RN   [1] {ECO:0000313|EMBL:KJS04922.1, ECO:0000313|Proteomes:UP000033681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS04922.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS04922.1}.
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DR   EMBL; LADZ01000054; KJS04922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NXC1; -.
DR   STRING; 1629721.VR77_10290; -.
DR   PATRIC; fig|1629721.3.peg.430; -.
DR   Proteomes; UP000033681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   177 AA;  19950 MW;  D091E8CD95310464 CRC64;
     MEIIKKFKTT FALLLMILVT VGFMYKQNTG LNVGEMAPDL KFNNPEGKQI ALSSLKGKVV
     LIDFWASWCV PCRRENPAVV KAYNMFKDKK FKNGKGFTVY GYSLDTNADL WKTAIEKDGL
     IWNNHTSDLK GWNSEGAQLY QVNSIPSNYL IDGDGKIIAK NLRGEALIDA LSKFEKK
//
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