ID A0A0H2M6H9_VARPD Unreviewed; 110 AA.
AC A0A0H2M6H9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN Name=trxA1 {ECO:0000313|EMBL:KLN58024.1};
GN Synonyms=trxA {ECO:0000313|EMBL:QGW82292.1};
GN ORFNames=GOQ09_12195 {ECO:0000313|EMBL:QGW82292.1}, VPARA_10360
GN {ECO:0000313|EMBL:KLN58024.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN58024.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN58024.1, ECO:0000313|Proteomes:UP000035170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN58024.1,
RC ECO:0000313|Proteomes:UP000035170};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QGW82292.1, ECO:0000313|Proteomes:UP000425817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSUSB {ECO:0000313|EMBL:QGW82292.1,
RC ECO:0000313|Proteomes:UP000425817};
RA Ne Ville C.J., Enright D., Hernandez I., Dodsworth J., Orwin P.M.;
RT "Hybrid Genome Assemblies of two High G+C Isolates from Undergraduate
RT Microbiology Courses.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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DR EMBL; JZWI01000005; KLN58024.1; -; Genomic_DNA.
DR EMBL; CP046622; QGW82292.1; -; Genomic_DNA.
DR RefSeq; WP_012747433.1; NZ_JZWI01000005.1.
DR AlphaFoldDB; A0A0H2M6H9; -.
DR GeneID; 67424806; -.
DR PATRIC; fig|34073.19.peg.1052; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000035170; Unassembled WGS sequence.
DR Proteomes; UP000425817; 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 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:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; 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 ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 28
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 36
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 110 AA; 12029 MW; 54CA0B87EB2483D5 CRC64;
MASDLIKHIS DSSFEADVLK SSQPVLVDYW AEWCGPCKMI APILDEVSTA YEGKLQIAKL
NVDENRDIPA KFGIRGIPTL MLFKDGQLAA TKVGAMSKAQ LTAFIDQQLA
//