ID S2XLX1_9BACL Unreviewed; 180 AA.
AC S2XLX1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Thioredoxin-like protein ykuU {ECO:0000313|EMBL:EPD52951.1};
GN ORFNames=HMPREF1210_01331 {ECO:0000313|EMBL:EPD52951.1};
OS Paenisporosarcina sp. HGH0030.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD52951.1, ECO:0000313|Proteomes:UP000014412};
RN [1] {ECO:0000313|EMBL:EPD52951.1, ECO:0000313|Proteomes:UP000014412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD52951.1,
RC ECO:0000313|Proteomes:UP000014412};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL Submitted (MAY-2013) 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:EPD52951.1}.
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DR EMBL; AGEQ01000006; EPD52951.1; -; Genomic_DNA.
DR RefSeq; WP_016427841.1; NZ_KE150421.1.
DR AlphaFoldDB; S2XLX1; -.
DR STRING; 1078085.HMPREF1210_01331; -.
DR PATRIC; fig|1078085.3.peg.1303; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_9; -.
DR Proteomes; UP000014412; 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:UP000014412}.
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; 20389 MW; 32A3233CD6C1A207 CRC64;
MTERMVGKQA PHFTMDAVLA DKSFGKVSLE ENMKQDKWTV LFFYPMDFTF VCPTEITAMS
DRYDEFEDLD AEIIGVSTDT IHTHLAWINT ARQDNGLGEL KYPLAADTNH VVSREYGVLI
EEEGIALRGL FIVNPEGEMQ YQTVFHNNIG RDVDETLRVL QALQTGGLCP ANWRPGQKTL
//
