ID F9RDL7_VIBSN Unreviewed; 242 AA.
AC F9RDL7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Peroxiredoxin family protein/glutaredoxin {ECO:0000313|EMBL:EGU33192.1};
GN ORFNames=VIBRN418_02941 {ECO:0000313|EMBL:EGU33192.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU33192.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU33192.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU33192.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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:EGU33192.1}.
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DR EMBL; AFWD01000056; EGU33192.1; -; Genomic_DNA.
DR RefSeq; WP_005595733.1; NZ_AFWD01000056.1.
DR AlphaFoldDB; F9RDL7; -.
DR eggNOG; COG0678; Bacteria.
DR eggNOG; COG0695; Bacteria.
DR Proteomes; UP000003627; 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; 26762 MW; 703B3533BD7A696F CRC64;
MFASKEGQAV PQVTFPTRQG DAWVNVTTDE LFKNKTVIVF SLPGAFTPTC SSSHLPRYNE
LYSVFKENGV DDILCVSVND TFVMNAWKAD QEAENITFIP DGNGDFTDGM GMLVDKNDLG
FGKRSWRYSM LVKNGVVEKM FIEEDVPGDP FKVSDADTML NYIAPEHKEQ ESITVFTKPG
CPFCMKAKQN LIDKGLNYEE VVLGKDATTV SLRAISGRTT VPQVFIGGKH IGGSEELETY
LG
//
