ID A0A0B2DCF0_9PSED Unreviewed; 108 AA.
AC A0A0B2DCF0; A0A0B3BSA6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=PT85_15775 {ECO:0000313|EMBL:KHO63936.1}, SAMN05421672_11684
GN {ECO:0000313|EMBL:SIR19940.1};
OS Pseudomonas flexibilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO63936.1, ECO:0000313|Proteomes:UP000030980};
RN [1] {ECO:0000313|EMBL:KHO63936.1, ECO:0000313|Proteomes:UP000030980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO63936.1,
RC ECO:0000313|Proteomes:UP000030980};
RA Shin S.-K., Yi H.;
RT "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIR19940.1, ECO:0000313|Proteomes:UP000186079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIR19940.1,
RC ECO:0000313|Proteomes:UP000186079};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; JTAK01000006; KHO63936.1; -; Genomic_DNA.
DR EMBL; FTMC01000016; SIR19940.1; -; Genomic_DNA.
DR RefSeq; WP_027590979.1; NZ_JTAK01000006.1.
DR AlphaFoldDB; A0A0B2DCF0; -.
DR STRING; 706570.PT85_15775; -.
DR PATRIC; fig|706570.3.peg.793; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000030980; Unassembled WGS sequence.
DR Proteomes; UP000186079; 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 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:UP000030980};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..108
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 27
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 34
FT /note="Contributes to redox potential value"
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 DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 108 AA; 11839 MW; CB81C70C8C141DED CRC64;
MSEFITNVSD ASFEQDVLQA DGPVLVDYWA EWCGPCKMIA PVLDEIAQTY QGKLKVCKLN
IDDNQETPPK YGVRGIPTLM LFKNGNVEAT KVGALSKSQL AAFLDANL
//
