ID Q30UB8_SULDN Unreviewed; 167 AA.
AC Q30UB8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Thiol peroxidase (Atypical 2-Cys peroxiredoxin) {ECO:0000313|EMBL:ABB43413.1};
DE EC=1.11.1.5 {ECO:0000313|EMBL:ABB43413.1};
GN OrderedLocusNames=Suden_0132 {ECO:0000313|EMBL:ABB43413.1};
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB43413.1, ECO:0000313|Proteomes:UP000002714};
RN [1] {ECO:0000313|EMBL:ABB43413.1, ECO:0000313|Proteomes:UP000002714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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DR EMBL; CP000153; ABB43413.1; -; Genomic_DNA.
DR RefSeq; WP_011371768.1; NC_007575.1.
DR AlphaFoldDB; Q30UB8; -.
DR STRING; 326298.Suden_0132; -.
DR KEGG; tdn:Suden_0132; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_2_7; -.
DR OrthoDB; 9781543at2; -.
DR Proteomes; UP000002714; Chromosome.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR CDD; cd03014; PRX_Atyp2cys; 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 InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 4: Predicted;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000313|EMBL:ABB43413.1};
KW Peroxidase {ECO:0000313|EMBL:ABB43413.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002714}.
FT DOMAIN 18..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 167 AA; 17416 MW; D88140E60E427FFA CRC64;
MATTKFKGTD VQLLGNQVNV GDKAPQITVV NSDGLGDVVV GGAQGHKQLI IVVPSLDTGV
CATETRNFNA KASSLNGVKP VIVSLDLPFA AGRFCSTEGI TNLTVTSDFR NKEFANAYGV
LLGGSVLAGV TCRAIFAVNE EGIVTYKEIV PEITEEPNYD AALAAVK
//
