ID C6A573_THESM Unreviewed; 192 AA.
AC C6A573;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Alkyl hydroperoxide reductase subunit c {ECO:0000313|EMBL:ACS90768.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:ACS90768.1};
GN OrderedLocusNames=TSIB_1717 {ECO:0000313|EMBL:ACS90768.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90768.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS90768.1, ECO:0000313|Proteomes:UP000009079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
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DR EMBL; CP001463; ACS90768.1; -; Genomic_DNA.
DR AlphaFoldDB; C6A573; -.
DR STRING; 604354.TSIB_1717; -.
DR KEGG; tsi:TSIB_1717; -.
DR eggNOG; arCOG00312; Archaea.
DR HOGENOM; CLU_042529_21_3_2; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
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 4: Predicted;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACS90768.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ACS90768.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT DOMAIN 5..162
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 192 AA; 21844 MW; 0EAF621EC899CE31 CRC64;
MKIMVMVGET VPDFEANAYF PEKDEIGKLR FSDYRGKWVI LAFYPADFTF VCPTELEELA
KYYEEFKKEG AEIISVSTDT AYVHKAWHDT SPSIKKIKYP MLADPAGKIS RLFGTYIEDE
GVSWRATFII DPDGKVVSMH IHDNSIGRSA KEILRMLRAS KYVREHPGQV CPASWEPGKE
TLKVSLDLVG KI
//
