ID A0A1J5IIP7_9GAMM Unreviewed; 242 AA.
AC A0A1J5IIP7;
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=Glutathione peroxidase {ECO:0000313|EMBL:OIP97009.1};
GN ORFNames=AUK56_00275 {ECO:0000313|EMBL:OIP97009.1};
OS Thiomicrospira sp. CG2_30_44_34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=1805397 {ECO:0000313|EMBL:OIP97009.1, ECO:0000313|Proteomes:UP000182935};
RN [1] {ECO:0000313|EMBL:OIP97009.1, ECO:0000313|Proteomes:UP000182935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_44_34 {ECO:0000313|EMBL:OIP97009.1};
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:OIP97009.1}.
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DR EMBL; MNZS01000003; OIP97009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5IIP7; -.
DR STRING; 1805397.AUK56_00275; -.
DR Proteomes; UP000182935; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000313|EMBL:OIP97009.1};
KW Peroxidase {ECO:0000313|EMBL:OIP97009.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 3..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 242 AA; 26496 MW; CAF67D605EF9D976 CRC64;
MENKQGQKVP SVVWPTRQNS EWVNVKSDDI FKGRTVVVFS LPGAFTPTCS SSHLPRYNEL
APVFFENGVD EIVCLSVNDT FVMNEWAKDQ ESTNVTLIPD GNGEFTEGMG MLVDKADLGF
GKRSWRYSML VKDGVVEKMF IEPNVPGDPF EVSDADTMLN YINPNAKPKK VATIFTKPGC
PFCAKAKAAL EDAGIEYEEI TISHSGVTSR TLRAVANADT VPQVFIEGKL IGGSDELAAY
LG
//
