ID F0GXB1_9FIRM Unreviewed; 231 AA.
AC F0GXB1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Antioxidant, AhpC/TSA family {ECO:0000313|EMBL:EGC81515.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:EGC81515.1};
GN ORFNames=HMPREF9290_0886 {ECO:0000313|EMBL:EGC81515.1};
OS Anaerococcus prevotii ACS-065-V-Col13.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=879305 {ECO:0000313|EMBL:EGC81515.1, ECO:0000313|Proteomes:UP000005286};
RN [1] {ECO:0000313|EMBL:EGC81515.1, ECO:0000313|Proteomes:UP000005286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-065-V-Col13 {ECO:0000313|EMBL:EGC81515.1,
RC ECO:0000313|Proteomes:UP000005286};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JAN-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:EGC81515.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEXM01000030; EGC81515.1; -; Genomic_DNA.
DR RefSeq; WP_004835428.1; NZ_AEXM01000030.1.
DR AlphaFoldDB; F0GXB1; -.
DR STRING; 879305.HMPREF9290_0886; -.
DR PATRIC; fig|879305.3.peg.1442; -.
DR eggNOG; COG1999; Bacteria.
DR Proteomes; UP000005286; Unassembled WGS sequence.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:EGC81515.1};
KW Peroxidase {ECO:0000313|EMBL:EGC81515.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005286};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..231
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038522049"
FT DOMAIN 73..221
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 21..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 25810 MW; E06D2530A1D94ACE CRC64;
MKNKILIAML FALTLTACGN TKNETKVEEK PETQQEEVKK DEVNKEEDKK DESKEADSQE
MKKEETESVD ASKAGAKMLP DFKATDQDGN GYSKEDIAKN DATVINLWFT GCSACIEEME
ALNDLATEIK GQEGVDFVSM CTDKDYDDST KEAYERIMKD KKPTYQALGV EYEGAMKEFL
ENIFVYPTTI VVDKNGNVIG DPIEGALTIP EQQEKLQENI NKAIESSKAS K
//
