ID A0A0J1D4S7_9BURK Unreviewed; 282 AA.
AC A0A0J1D4S7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:KLU27641.1};
GN ORFNames=EOS_03225 {ECO:0000313|EMBL:KLU27641.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU27641.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU27641.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU27641.1}.
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DR EMBL; AEJF01000021; KLU27641.1; -; Genomic_DNA.
DR RefSeq; WP_047845172.1; NZ_AEJF01000021.1.
DR AlphaFoldDB; A0A0J1D4S7; -.
DR PATRIC; fig|908627.4.peg.721; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF14561; TPR_20; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF48452; TPR-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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 282 AA; 30695 MW; 9A36E2AD21C096F6 CRC64;
MDTTLATFEQ DVIAASTLAP VLVDFWAPWC GPCKTLGPML ERLEAEGAGK WKLVKVNVDE
NPELAQHFQV RSIPHVVAFA DGRAVDQFIG VLSEGQLREF IDKLVPDGAE AERRAAHVAY
EAGDTDLAIG HIKATLALDP GYDEARLDLI EWLLAAGRTD EARAEDKLLS PKTTQGIDAR
YNALKTELDA ADAAASLPPA DALIDAVNAN PDDLEARFAL ANRLIAGRDY NGALEHLFAI
VTRDRSFMDD VGRKTMLSVF GLAAHQPEVV SQWRRKLSAA IN
//
