ID A0A248KH87_9ENTR Unreviewed; 141 AA.
AC A0A248KH87; A0A6G9RHA4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Thioredoxin TrxC {ECO:0000313|EMBL:ASG62899.1};
GN Name=trxC {ECO:0000313|EMBL:QIR26334.1};
GN ORFNames=CEW81_05730 {ECO:0000313|EMBL:ASG62899.1}, GY169_05720
GN {ECO:0000313|EMBL:QIR26334.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG62899.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG62899.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG62899.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIR26334.1, ECO:0000313|Proteomes:UP000503580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PO2S7 {ECO:0000313|EMBL:QIR26334.1,
RC ECO:0000313|Proteomes:UP000503580};
RA Singha K.M.;
RT "Whole genome PO2S7.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; CP022114; ASG62899.1; -; Genomic_DNA.
DR EMBL; CP050321; QIR26334.1; -; Genomic_DNA.
DR RefSeq; WP_064543411.1; NZ_CP050321.1.
DR AlphaFoldDB; A0A248KH87; -.
DR KEGG; kgo:CEW81_05730; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000197098; Chromosome.
DR Proteomes; UP000503580; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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 Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000197098};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..140
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 141 AA; 15863 MW; B0193B2F27C170AC CRC64;
MNTVCAHCQA LNRIPEERIN EAAKCGRCGE DLFDGDVINA TDSTLDKLLK DDLPVVVDFW
APWCGPCRNF APIFEDVAEE RSSTMRFVKV NTEAERELSA RFRIRSIPTI MIFKNGEVID
MLNGAVPKAP FESWLNEALQ A
//
