ID A0A420XEY7_9PAST Unreviewed; 87 AA.
AC A0A420XEY7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutaredoxin 1 {ECO:0000313|EMBL:RKR70827.1};
GN ORFNames=DES31_1837 {ECO:0000313|EMBL:RKR70827.1};
OS Otariodibacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Otariodibacter.
OX NCBI_TaxID=1032623 {ECO:0000313|EMBL:RKR70827.1, ECO:0000313|Proteomes:UP000280099};
RN [1] {ECO:0000313|EMBL:RKR70827.1, ECO:0000313|Proteomes:UP000280099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23800 {ECO:0000313|EMBL:RKR70827.1,
RC ECO:0000313|Proteomes:UP000280099};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {ECO:0000256|ARBA:ARBA00007787}.
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:RKR70827.1}.
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DR EMBL; RBJC01000010; RKR70827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420XEY7; -.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000280099; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR011902; GRXA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02183; GRXA; 1.
DR PANTHER; PTHR45694:SF28; GLUTAREDOXIN 1; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..69
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 87 AA; 9783 MW; 6D48E46F8E3D4943 CRC64;
MFVEIYGRLT CPYCVKAKTL AEKMKKELPD FDFEFINMIE KGISKEDLEP KVGGPVATVP
QIFLDNKHVG GSTDFVALVK EKFGIEL
//
