ID A0A085G7N8_9GAMM Unreviewed; 139 AA.
AC A0A085G7N8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Thioredoxin 2 {ECO:0000313|EMBL:KFC79733.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:KFC79733.1};
GN Name=trxC {ECO:0000313|EMBL:KFC79733.1};
GN ORFNames=GEAM_2885 {ECO:0000313|EMBL:KFC79733.1};
OS Ewingella americana ATCC 33852.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Ewingella.
OX NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC79733.1, ECO:0000313|Proteomes:UP000028640};
RN [1] {ECO:0000313|EMBL:KFC79733.1, ECO:0000313|Proteomes:UP000028640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC79733.1,
RC ECO:0000313|Proteomes:UP000028640};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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:KFC79733.1}.
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DR EMBL; JMPJ01000064; KFC79733.1; -; Genomic_DNA.
DR RefSeq; WP_034792689.1; NZ_JMPJ01000064.1.
DR AlphaFoldDB; A0A085G7N8; -.
DR STRING; 910964.GEAM_2885; -.
DR GeneID; 78382722; -.
DR eggNOG; COG3118; Bacteria.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000028640; Unassembled WGS sequence.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR049299; Thio2_N.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF40; THIOREDOXIN 2; 1.
DR Pfam; PF21352; Thio2_N; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Oxidoreductase {ECO:0000313|EMBL:KFC79733.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000028640};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..139
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 139 AA; 15363 MW; 017FB4D88DD30FB7 CRC64;
MNTICPSCQA TNRLPEDRIN DGAKCGRCGH ALFSGSVVHA TASTLDKYLQ DDLPVVIDFW
APWCGPCVSF APIFEDVAQE RAGKIRFIKV NTEAEPELSA RFRIRSIPTI MVFNEGKMVD
SLGGAMPKTP FNNWLNESL
//
