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Database: UniProt
Entry: A0A3M6Q3I8_9BURK
LinkDB: A0A3M6Q3I8_9BURK
Original site: A0A3M6Q3I8_9BURK 
ID   A0A3M6Q3I8_9BURK        Unreviewed;       302 AA.
AC   A0A3M6Q3I8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:RMW97763.1};
GN   Name=trxA {ECO:0000313|EMBL:RMW97763.1};
GN   ORFNames=EBQ25_09850 {ECO:0000313|EMBL:RMW97763.1};
OS   Allofranklinella schreckenbergeri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Allofranklinella.
OX   NCBI_TaxID=1076744 {ECO:0000313|EMBL:RMW97763.1, ECO:0000313|Proteomes:UP000267035};
RN   [1] {ECO:0000313|EMBL:RMW97763.1, ECO:0000313|Proteomes:UP000267035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML161473 {ECO:0000313|EMBL:RMW97763.1,
RC   ECO:0000313|Proteomes:UP000267035};
RA   Bernier A.-M., Bernard K.;
RT   "Comamonadaceae CDC group NO-1 genome sequencing and assembly.";
RL   Submitted (OCT-2018) 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:RMW97763.1}.
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DR   EMBL; RDQL01000014; RMW97763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6Q3I8; -.
DR   Proteomes; UP000267035; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 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   Reference proteome {ECO:0000313|Proteomes:UP000267035};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   302 AA;  33739 MW;  3A14CE472CF31103 CRC64;
     MIDVNLENFE TEVIQASMQT PVLVDFWAPW CGPCQTLGPI LEKLEVAYGG RFKLAKIDSD
     QQQQLAAMFG VRSIPTCVLM SQGQPVDGFM GALPESQLRA FLDKHLPEGP VLPVDDALST
     EDGAGEDDDL QSKLERLEKA VREQPDDEKA RFAYLRLLLE MGLEDEARAE FATVATLADG
     SLRYGAIRAW LEALEVARQA GDANARLQEL DAAIAADKRD FGARYQRAQL LLAHNQWTQA
     MDELLEILMR DRHWNEERAR KTYVAILEII EPPKPPVAEG QIPPEDPVVA SYRRRLSSVV
     LS
//
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