ID G5GKR9_9FIRM Unreviewed; 553 AA.
AC G5GKR9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Alkyl hydroperoxide reductase F subunit {ECO:0000313|EMBL:EHI54703.1};
GN ORFNames=HMPREF9333_02163 {ECO:0000313|EMBL:EHI54703.1};
OS Johnsonella ignava ATCC 51276.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Johnsonella.
OX NCBI_TaxID=679200 {ECO:0000313|EMBL:EHI54703.1, ECO:0000313|Proteomes:UP000003011};
RN [1] {ECO:0000313|EMBL:EHI54703.1, ECO:0000313|Proteomes:UP000003011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51276 {ECO:0000313|EMBL:EHI54703.1,
RC ECO:0000313|Proteomes:UP000003011};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Johnsonella ignava ATCC 51276.";
RL Submitted (AUG-2011) 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:EHI54703.1}.
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DR EMBL; ACZL01000045; EHI54703.1; -; Genomic_DNA.
DR AlphaFoldDB; G5GKR9; -.
DR STRING; 679200.HMPREF9333_02163; -.
DR PATRIC; fig|679200.3.peg.2276; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_5_4_9; -.
DR Proteomes; UP000003011; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017561; AhpF_homologue_put.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03143; AhpF_homolog; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003011};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 478..552
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT REGION 323..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 59650 MW; 5357A397094D4E91 CRC64;
MEKDKTLDIF YDVVIIGGGP AGLTAAIYLA RACYRVLVVE KEKFGGQITI TSEVVNYPGI
EHTNGSELTE TMRRQAQNFG AEFKLAEVIS INANADVKEV KTSSGTFKCF GILIATGARP
RMLGFEGEAR FRGHGVAYCA TCDGEFFTGK DVFVVGGGFA AAEEGVFLTK YAKHVYILVR
KPDFSCAKAV ADHAKNHEKI TVLTNTEVVR AEGDSLLRSI TYKNNITGEE TVYKAADGDT
FGIFVFAGYE PATELVKDIV ELDKSGYIVT DRNQKTSTDG VYAAGDVCIK ALRQVVTAVG
DGALAATELE KYASRLQKET GISPIRPVQS DKSTHGTVPS ENSSKTDAAN GNSGLFSPDM
LAQLEAVFEK MSGNVVLRLC LDERPVSSEL KEYMESLAAL TDKISISYED EVKSVTDAAP
FVKIISPDGS DSGLAFHGVP GGHEFTSFIL GIYNVSGPGQ AVPEDVLLKI KSINKKTAIK
IMVSLTCSVC PDLVVAAQRI AALNPLISAD IYDINHFEEL KDKYQIMSVP CMVINDGAPV
FGKKDIQQII ELI
//
