ID A0A3N4WLB0_9PAST Unreviewed; 242 AA.
AC A0A3N4WLB0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glutaredoxin-like protein {ECO:0000313|EMBL:RPE96486.1};
GN ORFNames=EDC49_0880 {ECO:0000313|EMBL:RPE96486.1};
OS Frederiksenia canicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Frederiksenia.
OX NCBI_TaxID=123824 {ECO:0000313|EMBL:RPE96486.1, ECO:0000313|Proteomes:UP000276901};
RN [1] {ECO:0000313|EMBL:RPE96486.1, ECO:0000313|Proteomes:UP000276901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25797 {ECO:0000313|EMBL:RPE96486.1,
RC ECO:0000313|Proteomes:UP000276901};
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 (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPE96486.1}.
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DR EMBL; RKQT01000001; RPE96486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4WLB0; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000276901; 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 4..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 242 AA; 26525 MW; 110A2B63E4FD074B CRC64;
MSATMEGKKV PEVTFHTRQG DQWVDVTTSS LFDNKTVVVF SLPGAFTPTC SSTHLPRYNE
LASEFKALGV DDIVCVSVND TFVMNAWKAD QESENVTVIP DGNGEFTAGM GMLVDKDDLG
FGKRSWRYSM LVKNGVVEKM FVEPNEPGDP FKVSDADTML KYIKPDWQAK PSVTIFTKPG
CPFCIKAKLL LDAKGLAYEE ILLGRDASTT SVRAITGKTS VPQIFIGGQH IGGSDDLEKY
FA
//
