ID A0A087N3Y7_9BACI Unreviewed; 180 AA.
AC A0A087N3Y7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:KFL43840.1};
GN ORFNames=CH76_04675 {ECO:0000313|EMBL:KFL43840.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43840.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL43840.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43840.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:KFL43840.1}.
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DR EMBL; JPUW01000007; KFL43840.1; -; Genomic_DNA.
DR RefSeq; WP_036143618.1; NZ_JPUW01000007.1.
DR AlphaFoldDB; A0A087N3Y7; -.
DR eggNOG; COG0450; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000029097; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029097}.
FT DOMAIN 4..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 52
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 180 AA; 20184 MW; F13A7F8CC7F5F77A CRC64;
MAERMVGKQA PAFEMQAVLA DKSFGKVSLE ENMKNDKWTV LFFYPMDFTF VCPTEITAMS
DRYDEFQDLD AEIIGVSTDT IHTHLAWIHT DRTDNGLGDL NYALAADTNH SVAKEYGVLI
EEEGIALRGL FIISPEGELK YQVVNHNDIG RDVDETLRVL QALQTGGLCP ANWRPGQKTL
//
