GenomeNet

Database: UniProt
Entry: K6XHU0_9ALTE
LinkDB: K6XHU0_9ALTE
Original site: K6XHU0_9ALTE 
ID   K6XHU0_9ALTE            Unreviewed;       246 AA.
AC   K6XHU0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=GARC_3265 {ECO:0000313|EMBL:GAC20224.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC20224.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC20224.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC20224.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAC20224.1}.
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DR   EMBL; BAEO01000049; GAC20224.1; -; Genomic_DNA.
DR   RefSeq; WP_007621953.1; NZ_BAEO01000049.1.
DR   AlphaFoldDB; K6XHU0; -.
DR   STRING; 493475.GARC_3265; -.
DR   eggNOG; COG0678; Bacteria.
DR   eggNOG; COG0695; Bacteria.
DR   OrthoDB; 9800621at2; -.
DR   Proteomes; UP000006327; 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; 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; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327}.
FT   DOMAIN          8..172
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        54
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ   SEQUENCE   246 AA;  26672 MW;  A0655B230C456F5D CRC64;
     MSNPNFADKS GQAVPQCSFA ARVNDEWVKL TTDELFKGKT VVVFSLPGAF TPTCSSTHLP
     RYNELAKTFK ANGVDEIICV SVNDTFVMNA WAADQESDNV TLIPDGNGDF TNGMGLLVDK
     SEIGFGKRSW RYSMLVKDGV VDKMFIEPDL PGDPFEVSDA DTMLAYVAPE AKASVATAIL
     TKPGCPFCAK AKKLLDEKGF EYEELVMGKE VSFTSLKALS GNESWPQVFI GGKLIGGSDD
     LEAYFA
//
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