ID A0A1J4RLL9_9ARCH Unreviewed; 187 AA.
AC A0A1J4RLL9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:OIN87944.1};
GN ORFNames=AUJ50_02070 {ECO:0000313|EMBL:OIN87944.1};
OS Candidatus Aenigmarchaeota archaeon CG1_02_38_14.
OC Archaea; Candidatus Aenigmarchaeota.
OX NCBI_TaxID=1803500 {ECO:0000313|EMBL:OIN87944.1, ECO:0000313|Proteomes:UP000182362};
RN [1] {ECO:0000313|EMBL:OIN87944.1, ECO:0000313|Proteomes:UP000182362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_38_14 {ECO:0000313|EMBL:OIN87944.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIN87944.1}.
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DR EMBL; MNUF01000028; OIN87944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4RLL9; -.
DR Proteomes; UP000182362; Unassembled WGS sequence.
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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 187 AA; 21100 MW; 15DAE8D8720A9093 CRC64;
MVKINEKAPD FREDAFIDGK MKKISLSGYK GKWVVLFFYP ADFTFVCPTE LGELADKYEK
FKELGAEIIS VSTDTAYVHK AWHDNSETIK KIKFPMLSDP ARRVAASYGT LIENEGLSLR
ATFLINPDGV IKAYEFHDND IGRSSHELIR KLEAAKFVSE HKGQVCPINW MPGEKTLKPG
LDLVGKI
//